Active sites-ENZYMES
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This document discusses prosthetic groups, which are non-amino acid components that are covalently linked to proteins and required for their biological activity. Prosthetic groups can be organic or inorganic molecules like vitamins, metals, or lipids. The document also outlines some key factors that influence enzyme activity, such as temperature, pH, enzyme concentration, and substrate concentration.
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MECHANISM OF ENZYME ACTION
An enzyme attracts substrates to its active site, catalyzes the chemical reaction by which products are formed, and then allows the products to dissociate (separate from the enzyme surface). The combination formed by an enzyme and its substrates is called the enzyme-substrate complex.
Bisubstrate
This document discusses bisubstrate reactions, which involve two substrates and produce two products. Approximately 60% of biochemical reactions are bisubstrate reactions. They can be transferase reactions, where a functional group is transferred between substrates, or oxidation-reduction reactions. Bisubstrate reactions fall into two categories: sequential reactions, where substrates bind sequentially before products are released; and ping pong reactions, where an intermediate enzyme form is produced after the first substrate reaction. Common examples of each type of bisubstrate reaction are provided.
Chapter-6 enzymes - Biochemistry
Enzymes are biological catalysts that greatly accelerate chemical reactions in living organisms. They are typically proteins that precisely bind substrates in their active sites, properly orienting them and bringing reactive groups close together. This organization lowers the activation energy barrier for reactions. Enzymes achieve catalysis by stabilizing transition state interactions even more than ground state interactions, through complementary shapes and interactions optimized for the transition state geometry. As a result, enzymes can tremendously increase reaction rates without disrupting chemical equilibrium.
Multifunctional enzymes
Multifunctional enzymes contain two or more distinct catalytic activities located in a single polypeptide chain. Fatty acid synthase is a multifunctional enzyme that synthesizes fatty acids through seven distinct enzymatic activities located on three functional domains. DNA polymerase is another multifunctional enzyme that synthesizes DNA and proofreads for errors through its polymerase and exonuclease activities.
Allosteric inhibition
The document discusses allosteric regulation of enzymes. Allosteric enzymes can exist in two conformations - an active form which can bind substrate and an inactive form which binds inhibitors. Effectors like substrates or inhibitors binding at allosteric sites can stabilize one form over the other. One example discussed is aspartate transcarbamoylase which regulates pyrimidine synthesis and shows cooperative substrate binding and allosteric regulation by ATP and CTP.
Enzymes and their properties
Enzymes are protein molecules that act as catalysts for chemical reactions in living organisms. They speed up reactions by lowering their activation energy but are not used up in the process. Enzymes have specific active sites that substrates bind to, and use lock-and-key or induced-fit mechanisms to catalyze reactions. The rate of enzymatic reactions depends on substrate concentration according to Michaelis-Menten kinetics, characterized by the parameters Km and Vmax. Enzymes are essential for many biological functions and processes and have important industrial applications like food production, biofuels, and cleaning products.
Enzymes
Enzymes are biological catalysts, mainly proteins, that speed up chemical reactions in organisms. The first enzyme, diastase, was discovered in 1833 by Payen, and in 1897 Buchner found that yeast cells could ferment sugar without being alive. Enzymes work by lowering the activation energy of reactions, bringing substrates together correctly, and forming enzyme-substrate complexes. They are classified based on the type of reaction catalyzed, such as hydrolases which use water or lyases which remove groups non-hydrolytically. Enzymes have many uses including in food processing, detergents, and paper production.
CHEMISTRY OF ENZYMES
This document provides an overview of enzymes, including their chemistry, nomenclature, classification, mechanisms of action, and factors that affect enzyme activity. It discusses how enzymes are proteins that act as biological catalysts, lowering the activation energy of biochemical reactions. Enzymes are classified according to the type of chemical reactions they catalyze into six main classes: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. The document also covers enzyme kinetics, regulation, diagnostic and therapeutic uses of enzymes.
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Trypsin, chymotripsin & urease
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MECHANISM OF ENZYME ACTION
An enzyme attracts substrates to its active site, catalyzes the chemical reaction by which products are formed, and then allows the products to dissociate (separate from the enzyme surface). The combination formed by an enzyme and its substrates is called the enzyme-substrate complex.
Bisubstrate
This document discusses bisubstrate reactions, which involve two substrates and produce two products. Approximately 60% of biochemical reactions are bisubstrate reactions. They can be transferase reactions, where a functional group is transferred between substrates, or oxidation-reduction reactions. Bisubstrate reactions fall into two categories: sequential reactions, where substrates bind sequentially before products are released; and ping pong reactions, where an intermediate enzyme form is produced after the first substrate reaction. Common examples of each type of bisubstrate reaction are provided.
Chapter-6 enzymes - Biochemistry
Enzymes are biological catalysts that greatly accelerate chemical reactions in living organisms. They are typically proteins that precisely bind substrates in their active sites, properly orienting them and bringing reactive groups close together. This organization lowers the activation energy barrier for reactions. Enzymes achieve catalysis by stabilizing transition state interactions even more than ground state interactions, through complementary shapes and interactions optimized for the transition state geometry. As a result, enzymes can tremendously increase reaction rates without disrupting chemical equilibrium.
Multifunctional enzymes
Multifunctional enzymes contain two or more distinct catalytic activities located in a single polypeptide chain. Fatty acid synthase is a multifunctional enzyme that synthesizes fatty acids through seven distinct enzymatic activities located on three functional domains. DNA polymerase is another multifunctional enzyme that synthesizes DNA and proofreads for errors through its polymerase and exonuclease activities.
Allosteric inhibition
The document discusses allosteric regulation of enzymes. Allosteric enzymes can exist in two conformations - an active form which can bind substrate and an inactive form which binds inhibitors. Effectors like substrates or inhibitors binding at allosteric sites can stabilize one form over the other. One example discussed is aspartate transcarbamoylase which regulates pyrimidine synthesis and shows cooperative substrate binding and allosteric regulation by ATP and CTP.
Enzymes and their properties
Enzymes are protein molecules that act as catalysts for chemical reactions in living organisms. They speed up reactions by lowering their activation energy but are not used up in the process. Enzymes have specific active sites that substrates bind to, and use lock-and-key or induced-fit mechanisms to catalyze reactions. The rate of enzymatic reactions depends on substrate concentration according to Michaelis-Menten kinetics, characterized by the parameters Km and Vmax. Enzymes are essential for many biological functions and processes and have important industrial applications like food production, biofuels, and cleaning products.
Enzymes
Enzymes are biological catalysts, mainly proteins, that speed up chemical reactions in organisms. The first enzyme, diastase, was discovered in 1833 by Payen, and in 1897 Buchner found that yeast cells could ferment sugar without being alive. Enzymes work by lowering the activation energy of reactions, bringing substrates together correctly, and forming enzyme-substrate complexes. They are classified based on the type of reaction catalyzed, such as hydrolases which use water or lyases which remove groups non-hydrolytically. Enzymes have many uses including in food processing, detergents, and paper production.
CHEMISTRY OF ENZYMES
This document provides an overview of enzymes, including their chemistry, nomenclature, classification, mechanisms of action, and factors that affect enzyme activity. It discusses how enzymes are proteins that act as biological catalysts, lowering the activation energy of biochemical reactions. Enzymes are classified according to the type of chemical reactions they catalyze into six main classes: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. The document also covers enzyme kinetics, regulation, diagnostic and therapeutic uses of enzymes.
Active site of enzyme
Active sites of the enzyme is that point where substrate molecule bind for the chemical reaction. It is generally found on the surface of enzyme and in some enzyme it is a “Pit” like structure
The active site is a three-dimensional cleft formed by groups that come from different parts of the amino acid sequence
The active site takes up a relatively small part of the total volume of an enzyme
Active sites are clefts or crevices
Substrates are bound to enzymes by multiple weak attractions.
The specificity of binding depends on the precisely defined arrangement of atoms in an active site.
Mechanism of enzyme action
Presentation given by Dr. Karthikeyan at Department of Biochemistry, Maulana Azad Medical College on 04.04.2013.
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This document discusses enzymes, including their definition, IUB nomenclature system, mechanisms of action, and types of inhibition. It defines enzymes as soluble, colloidal organic catalysts formed by living cells that are specific, protein in nature, and inactivated by heat. The IUB system provides unique names and code numbers for enzymes. Mechanisms of action include the lock-and-key and induced fit models. Inhibition can be reversible, irreversible, or allosteric depending on whether the inhibitor binds noncovalently or covalently and where it binds on the enzyme.
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Allosteric enzymes and their regulation
This document discusses allosteric enzymes and their regulation. Allosteric enzymes have additional sites called allosteric sites that regulate enzyme activity. Enzyme activity can be activated or inhibited by metabolites interacting with these allosteric sites, known as allosteric regulation. There are two main models that explain allosteric regulation: the concerted model and sequential model. Allosteric regulation can be homotropic, where the substrate regulates the enzyme, or heterotropic, where a non-substrate regulatory molecule activates or inhibits the enzyme. Examples of each type of allosteric regulation are given.
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1. Cofactors and coenzymes assist enzymes in catalyzing reactions. Cofactors are tightly bound to enzymes while coenzymes bind reversibly.
2. Common coenzymes include NAD+, FAD, coenzyme A, biotin, thiamine pyrophosphate, and pyridoxal phosphate. They transfer elements like electrons, acyl groups, and amino groups between reactions.
3. Coenzymes can be classified as metabolite or vitamin-derived. Vitamin-derived coenzymes include NAD+, FAD, coenzyme A, and others that derive from vitamins like niacin, riboflavin, pantot
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Enzymes catalyze reactions by lowering the activation energy needed to reach the transition state. They provide an alternate reaction pathway with a lower energy barrier compared to uncatalyzed reactions. The active site of an enzyme chemically facilitates catalysis by stabilizing the transition state of the reaction. It acts as a flexible template that stabilizes the substrate in its transition state, accelerating the reaction. The active site also provides catalytic groups that increase the probability of transition state formation. Common mechanisms of enzyme action include the lock and key model and induced fit model. Enzyme catalysis is achieved through proximity effects, acid-base catalysis using functional groups to enhance transition state formation, substrate strain, and sometimes covalent catalysis where the
Measurement of ENZYME ACTIVITY
Enzymes are biological catalysts that speed up chemical reactions without being consumed. Their activity can be measured by determining the amount of substrate converted to product per unit time. There are two main types of enzyme assays: continuous assays that measure reaction rates over time, and discontinuous assays that take samples at intervals to measure substrate/product levels. Common techniques to measure enzyme activity include spectrophotometry, fluorescence spectroscopy, chromatography, and radiometric methods. Spectrophotometry is often used to examine light absorption of substrates and products in the ultraviolet-visible range.
Classification of enzymes
This document discusses the classification of enzymes. Enzymes are classified into seven major classes based on the type of chemical reaction they catalyze: oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases, and translocases. Each enzyme is assigned a four-digit Enzyme Commission (EC) number that identifies its class and subclass. For example, EC 2.7.1.1 indicates that hexokinase is a transferase that transfers phosphate groups. The systematic classification of enzymes by reaction type allows for a standardized naming system and identification codes.
Protein Purification
This document provides an overview of various protein purification techniques, including:
- Chromatography methods like affinity chromatography, ion exchange chromatography, size exclusion chromatography, and hydrophobic interaction chromatography.
- Key steps in protein purification like cell lysis, centrifugation, assaying fractions for protein and activity, and monitoring purity with SDS-PAGE gels.
- Considerations for each chromatography method like matrix selection, binding capacities, and driving forces.
- Emerging techniques like capillary electrochromatography and multi-dimensional separations.
Biochemistry lecture notes enzymes
Enzymes are protein catalysts that greatly increase the rates of biochemical reactions. They achieve this by lowering the activation energy of reactions. Enzymes are highly specific and only catalyze one or a small number of reaction types. The enzyme binds to its substrate at its active site, and uses functional groups to facilitate the reaction, ultimately releasing the product. Many factors can influence an enzyme's activity level, including its concentration, the substrate concentration, temperature, pH, and the presence of inhibitors.
Mechanisms action of enzymes
Enzymes lower the activation energy of reactions by several mechanisms:
1. Enzymes orient the substrate in a strained transition state that more closely resembles the activation energy.
2. Metal ions and cofactors in metalloenzymes help orient substrates for reaction.
3. Specific amino acids in the active site preferentially bind to and stabilize the higher energy transition state.
4. Bringing substrates close together in multienzyme complexes or keeping reaction intermediates channeled increases reaction rates.
Bisubstrate reactions enzyme kinetics
This document discusses two types of bisubstrate reactions: sequential or single-displacement reactions and ping-pong or double-displacement reactions. Sequential reactions involve both substrates binding to the enzyme before products are released, and can be ordered or random. Ping-pong reactions involve one substrate binding and being modified, then releasing one product before the second substrate binds and the second product is released, regenerating the original enzyme. Examples of each type of reaction are provided to illustrate the mechanisms.
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This document provides an overview of enzymes and enzyme kinetics taught in the Principles of Biochemistry course (HFB324) by Dr. Siham Gritly. It defines key enzyme terms and concepts, describes enzyme classification systems, the components and localization of enzymes in the body, and models of enzyme catalysis including active sites and enzyme-substrate binding. It also explains Michaelis-Menten kinetics and how various factors influence the velocity of enzyme reactions such as substrate concentration, temperature, and inhibitors.
Regulation of enzyme activity
1. Enzyme activity can be regulated through several mechanisms including allosteric regulation, feedback inhibition, proenzymes, and protein modification.
2. Allosteric enzymes have effector molecules that bind and induce a conformational change that increases or decreases enzyme activity. Feedback inhibition occurs when a metabolic end product inhibits an earlier enzyme.
3. Proenzymes are inactive precursors that are activated by proteolytic cleavage. Protein modification like phosphorylation can also regulate enzymes by changing their structure.
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Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They have specific three-dimensional structures with active sites that bind substrates and catalyze their conversion to products. There are six main enzyme classes defined by their catalyzed reaction types. Enzyme activity is affected by factors like substrate and enzyme concentration, pH, temperature, and inhibitors. Enzymes lower activation energy and use lock-and-key or induced-fit binding to catalyze reactions efficiently through transition states. Many require cofactors like vitamins and metal ions to function. Enzyme kinetics describe how rates change with conditions and inhibition mechanisms. Enzymes are essential to all living functions but some inhibitors like nerve gases are toxic.
ENZYMES
This document provides information about enzymes including their history, characteristics, classification, and mechanisms of action. Some key points:
- Enzymes are organic biocatalysts that accelerate chemical reactions by lowering the activation energy. They are not consumed by the reactions they catalyze.
- The term "enzyme" was first used in the 19th century to describe digestion processes. Important early discoveries included identifying enzymes responsible for starch digestion and fermentation.
- Enzymes are usually proteins but can also be RNA. They are highly specific and act as catalysts by lowering the activation energy of reactions through transition state stabilization.
- The International Union of Biochemistry and Molecular Biology (IUBMB)
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The document discusses various types of post-translational modifications (PTMs) of proteins. It describes how PTMs are necessary for normal protein functioning by affecting stability, activity, localization, and signaling. It provides examples of common PTMs like phosphorylation, glycosylation, acetylation, lipidation, disulfide bonding, and ubiquitination. It also discusses protein folding, subunit aggregation, and protein splicing - key processes in protein maturation that occur after translation. PTMs are an important mechanism for regulating protein structure and function after synthesis.
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Active sites of the enzyme is that point where substrate molecule bind for the chemical reaction. It is generally found on the surface of enzyme and in some enzyme it is a “Pit” like structure
The active site is a three-dimensional cleft formed by groups that come from different parts of the amino acid sequence
The active site takes up a relatively small part of the total volume of an enzyme
Active sites are clefts or crevices
Substrates are bound to enzymes by multiple weak attractions.
The specificity of binding depends on the precisely defined arrangement of atoms in an active site.
Mechanism of enzyme action
Presentation given by Dr. Karthikeyan at Department of Biochemistry, Maulana Azad Medical College on 04.04.2013.
Enzyme
This document discusses enzymes, including their definition, IUB nomenclature system, mechanisms of action, and types of inhibition. It defines enzymes as soluble, colloidal organic catalysts formed by living cells that are specific, protein in nature, and inactivated by heat. The IUB system provides unique names and code numbers for enzymes. Mechanisms of action include the lock-and-key and induced fit models. Inhibition can be reversible, irreversible, or allosteric depending on whether the inhibitor binds noncovalently or covalently and where it binds on the enzyme.
Multienzyme System.pdf
Multienzyme System: A complex of enzymes within a cell that form a reaction sequence of a biochemical pathway so that the product of the first enzyme reaction is transferred directly to the next enzyme and immediately undergoes a second reaction, and so on.
Regulatory and allosteric enzymes and allostrerism
This ppt describes the overview of enzyme regulation and Allosterism. Presented since October 23,2017GC at Addis Ababa University, School of Medicine, Department of medical biochemistry.
myoglobin
Myoglobin is a protein found in muscle tissue that binds oxygen. It was the first protein whose three-dimensional structure was determined using X-ray crystallography in the 1950s-60s. Myoglobin facilitates oxygen transport within muscles through reversible binding of oxygen to an iron-containing heme group. It stores oxygen to help meet rapid energy demands in muscle cells and prevents accumulation of toxic nitric oxide.
Allosteric enzymes and their regulation
This document discusses allosteric enzymes and their regulation. Allosteric enzymes have additional sites called allosteric sites that regulate enzyme activity. Enzyme activity can be activated or inhibited by metabolites interacting with these allosteric sites, known as allosteric regulation. There are two main models that explain allosteric regulation: the concerted model and sequential model. Allosteric regulation can be homotropic, where the substrate regulates the enzyme, or heterotropic, where a non-substrate regulatory molecule activates or inhibits the enzyme. Examples of each type of allosteric regulation are given.
Cofactor and Coenzyme.ppt
1. Cofactors and coenzymes assist enzymes in catalyzing reactions. Cofactors are tightly bound to enzymes while coenzymes bind reversibly.
2. Common coenzymes include NAD+, FAD, coenzyme A, biotin, thiamine pyrophosphate, and pyridoxal phosphate. They transfer elements like electrons, acyl groups, and amino groups between reactions.
3. Coenzymes can be classified as metabolite or vitamin-derived. Vitamin-derived coenzymes include NAD+, FAD, coenzyme A, and others that derive from vitamins like niacin, riboflavin, pantot
3 enzyme kinetics
Enzymes catalyze reactions by lowering the activation energy needed to reach the transition state. They provide an alternate reaction pathway with a lower energy barrier compared to uncatalyzed reactions. The active site of an enzyme chemically facilitates catalysis by stabilizing the transition state of the reaction. It acts as a flexible template that stabilizes the substrate in its transition state, accelerating the reaction. The active site also provides catalytic groups that increase the probability of transition state formation. Common mechanisms of enzyme action include the lock and key model and induced fit model. Enzyme catalysis is achieved through proximity effects, acid-base catalysis using functional groups to enhance transition state formation, substrate strain, and sometimes covalent catalysis where the
Measurement of ENZYME ACTIVITY
Enzymes are biological catalysts that speed up chemical reactions without being consumed. Their activity can be measured by determining the amount of substrate converted to product per unit time. There are two main types of enzyme assays: continuous assays that measure reaction rates over time, and discontinuous assays that take samples at intervals to measure substrate/product levels. Common techniques to measure enzyme activity include spectrophotometry, fluorescence spectroscopy, chromatography, and radiometric methods. Spectrophotometry is often used to examine light absorption of substrates and products in the ultraviolet-visible range.
Classification of enzymes
This document discusses the classification of enzymes. Enzymes are classified into seven major classes based on the type of chemical reaction they catalyze: oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases, and translocases. Each enzyme is assigned a four-digit Enzyme Commission (EC) number that identifies its class and subclass. For example, EC 2.7.1.1 indicates that hexokinase is a transferase that transfers phosphate groups. The systematic classification of enzymes by reaction type allows for a standardized naming system and identification codes.
Protein Purification
This document provides an overview of various protein purification techniques, including:
- Chromatography methods like affinity chromatography, ion exchange chromatography, size exclusion chromatography, and hydrophobic interaction chromatography.
- Key steps in protein purification like cell lysis, centrifugation, assaying fractions for protein and activity, and monitoring purity with SDS-PAGE gels.
- Considerations for each chromatography method like matrix selection, binding capacities, and driving forces.
- Emerging techniques like capillary electrochromatography and multi-dimensional separations.
Biochemistry lecture notes enzymes
Enzymes are protein catalysts that greatly increase the rates of biochemical reactions. They achieve this by lowering the activation energy of reactions. Enzymes are highly specific and only catalyze one or a small number of reaction types. The enzyme binds to its substrate at its active site, and uses functional groups to facilitate the reaction, ultimately releasing the product. Many factors can influence an enzyme's activity level, including its concentration, the substrate concentration, temperature, pH, and the presence of inhibitors.
Mechanisms action of enzymes
Enzymes lower the activation energy of reactions by several mechanisms:
1. Enzymes orient the substrate in a strained transition state that more closely resembles the activation energy.
2. Metal ions and cofactors in metalloenzymes help orient substrates for reaction.
3. Specific amino acids in the active site preferentially bind to and stabilize the higher energy transition state.
4. Bringing substrates close together in multienzyme complexes or keeping reaction intermediates channeled increases reaction rates.
Bisubstrate reactions enzyme kinetics
This document discusses two types of bisubstrate reactions: sequential or single-displacement reactions and ping-pong or double-displacement reactions. Sequential reactions involve both substrates binding to the enzyme before products are released, and can be ordered or random. Ping-pong reactions involve one substrate binding and being modified, then releasing one product before the second substrate binds and the second product is released, regenerating the original enzyme. Examples of each type of reaction are provided to illustrate the mechanisms.
6 enzymes
This document provides an overview of enzymes and enzyme kinetics taught in the Principles of Biochemistry course (HFB324) by Dr. Siham Gritly. It defines key enzyme terms and concepts, describes enzyme classification systems, the components and localization of enzymes in the body, and models of enzyme catalysis including active sites and enzyme-substrate binding. It also explains Michaelis-Menten kinetics and how various factors influence the velocity of enzyme reactions such as substrate concentration, temperature, and inhibitors.
Regulation of enzyme activity
1. Enzyme activity can be regulated through several mechanisms including allosteric regulation, feedback inhibition, proenzymes, and protein modification.
2. Allosteric enzymes have effector molecules that bind and induce a conformational change that increases or decreases enzyme activity. Feedback inhibition occurs when a metabolic end product inhibits an earlier enzyme.
3. Proenzymes are inactive precursors that are activated by proteolytic cleavage. Protein modification like phosphorylation can also regulate enzymes by changing their structure.
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Antigen antibody interactions play important role in immunological assays which help in detection of disease.Such interaction are of various types e.g.Precipitation,Flocculation, Agglutination, Complement fixation, ELISA,RIA, Immunoflourescence,Immunoprecipitation.
Enzymes
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They have specific three-dimensional structures with active sites that bind substrates and catalyze their conversion to products. There are six main enzyme classes defined by their catalyzed reaction types. Enzyme activity is affected by factors like substrate and enzyme concentration, pH, temperature, and inhibitors. Enzymes lower activation energy and use lock-and-key or induced-fit binding to catalyze reactions efficiently through transition states. Many require cofactors like vitamins and metal ions to function. Enzyme kinetics describe how rates change with conditions and inhibition mechanisms. Enzymes are essential to all living functions but some inhibitors like nerve gases are toxic.
ENZYMES
This document provides information about enzymes including their history, characteristics, classification, and mechanisms of action. Some key points:
- Enzymes are organic biocatalysts that accelerate chemical reactions by lowering the activation energy. They are not consumed by the reactions they catalyze.
- The term "enzyme" was first used in the 19th century to describe digestion processes. Important early discoveries included identifying enzymes responsible for starch digestion and fermentation.
- Enzymes are usually proteins but can also be RNA. They are highly specific and act as catalysts by lowering the activation energy of reactions through transition state stabilization.
- The International Union of Biochemistry and Molecular Biology (IUBMB)
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Peptides and proteins are polymers of amino acids. Their structure and function depend on the nature, sequence, and spatial arrangement of amino acids. Peptides generally have fewer than 100 amino acids, while proteins have 100 or more. Many peptides are formed by protein breakdown. Examples of physiologically active peptides include glutathione, bradykinin, angiotensin, vasopressin, oxytocin, and TRH. Proteins perform functions like maintaining pH and osmotic balance. They also include enzymes, hormones, and structural components of tissues.
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This document summarizes various types of post-translational modifications that proteins undergo, including acetylation, phosphorylation, methylation, prenylation, hydroxylation, amidation, and carboxylation. It provides examples of each modification and discusses how they are involved in activating proteins or regulating their function and activity. The mechanisms of N-linked and O-linked glycosylation are also summarized, including how oligosaccharides are attached to proteins via glycosidic bonds in the ER and Golgi apparatus.
Protein Folding
This document discusses protein structure and folding. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structure involves folding into alpha helices or beta sheets. Tertiary structure is the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure refers to interactions between multiple polypeptide chains in a protein. The document also discusses protein folding, denaturation, and misfolding, noting that many neurodegenerative diseases are associated with misfolded protein aggregates.
1s.ENZYMES.pptx
Enzymes are protein catalysts that accelerate chemical reactions in living organisms. They facilitate reactions by lowering the activation energy needed. Enzymes achieve specificity through their active sites, which are complementary in shape and chemical properties to their substrates. Factors like temperature, pH, and inhibitors can impact an enzyme's activity. There are several mechanisms of enzyme action and regulation, including competitive and non-competitive inhibition, as well as allosteric regulation through effectors binding at distinct sites. Precise control of enzymes is crucial for metabolic processes in cells and organisms.
Protein folding
The document discusses protein folding, which is the process by which proteins achieve their functional three-dimensional structure from their linear amino acid sequence. It describes the different levels of protein structure, including primary, secondary, tertiary, and quaternary structure. The folding process depends on factors like temperature, pH, and molecular chaperones, which assist in protein folding. Proper folding is required for proteins to carry out their functions in the cell.
digestion and absorption of proteins.pptx
digestion and absorption of proteins
how proteins are digested and how they are absorbed in our body are discussed here
Similar to Active sites-ENZYMES (20)
Rational design of non- covalently and covalently binding.pptx
Rational design of non- covalently and covalently binding.pptx
Protein Folding-Self Assembly & Role of Chaperones in Protein Assembly.
Protein Folding-Self Assembly & Role of Chaperones in Protein Assembly.
More from KARTHIK REDDY C A
Types of Food packaging materials .pptx
Packaging plays an important role in protecting foods and influencing their storage life and marketability. It acts as a barrier between foods and the environment. Different types of packaging materials include paper, plastic, wood, and more. Materials must have properties like being non-toxic, providing moisture and gas barriers, and allowing for visibility and easy disposal. Packaging can be classified by the stage of distribution and includes primary, secondary, and tertiary containers. New intelligent and biodegradable packaging technologies also aim to provide information on food quality while reducing environmental impact.
Solid-waste-management .pptx
This document discusses solid waste and its management. It defines different types of solid waste like municipal waste, hazardous waste, and hospital waste. Municipal solid waste consists of household waste, construction debris, and other sanitation waste. Hazardous waste from industries and hospitals can be toxic. Hospital waste includes sharps, soiled waste, and infectious materials. The document also outlines the various causes and effects of improper solid waste management, such as health hazards and environmental impacts. It promotes following the 4R approach of reduce, reuse, recycle, and refuse to better manage solid waste.
QUALITY-ASSURANCE-AND-FOOD -SAFETY .pptx
This document discusses quality assurance and food safety. It defines quality as meeting requirements and fitness for use. Quality control evaluates the final product while quality assurance aims to prevent issues through systematic planning across the production process. Food safety ensures food will not harm consumers, but safety is difficult to observe and issues like contamination can impact health, marketing and trade. Responsibilities of quality assurance include ensuring quality policies are followed, identifying standard operating procedures, and monitoring operations for compliance. Quality control is responsible for testing raw materials, in-process items, and finished products. The document also discusses controlling quality variation through raw material specifications, in-process monitoring, and manufacturing condition monitoring.
Preservation of Food and feed using irradiation .pptx
Food irradiation is a process that exposes food to controlled sources of ionizing radiation to reduce microbes, destroy pathogens, and extend shelf life. There are three approved radiation sources: gamma rays from cobalt-60, x-rays from electron beams, and electron beams themselves. Irradiation kills bacteria and other microbes by damaging their DNA/RNA without increasing food temperature or altering appearance/taste. Common irradiated foods include fruits, vegetables, spices, meat and seafood. Benefits are longer shelf life and reduced foodborne illness without compromising safety.
Food sanitation .pptx
This document discusses various types of food contaminants including biological, physical, and chemical contaminants. It provides examples of each type and methods for preventing contamination. Specifically, it emphasizes the importance of proper handwashing, cleaning and sanitizing surfaces and equipment, separating raw and ready-to-eat foods during storage and preparation, and avoiding time/temperature abuse by keeping foods out of the danger zone between 40-140°F. Potentially hazardous foods that require special handling are also identified.
Food Safety And Quality Assurance K R.pptx
This document discusses food safety and quality assurance. It notes that an estimated 600 million people fall ill from contaminated food each year, resulting in over 420,000 deaths. Ensuring food safety is important to prevent disease and malnutrition. Food quality assurance systems aim to maintain standards for raw materials and finished products, produce accurate information for intended purposes, and evaluate performance against requirements to satisfy customers. International food supply chains present challenges for achieving consistent food quality standards.
Food Preservation .pptx
This document discusses various methods of food preservation including prevention of microbial decomposition, prevention of self-decomposition, and prevention of damage from insects and animals. It describes methods such as asepsis, removal of microorganisms, use of temperature through processes like canning and drying, use of chemical preservatives, and irradiation. Specific techniques are outlined, such as packaging, sanitation, filtration, centrifugation, washing, trimming, and maintenance of anaerobic conditions.
Food preservation by chemicals .pptx
Chemical preservatives are used to prevent food spoilage caused by microorganisms and extend shelf life. They are classified as class I or class II. Class I preservatives like salt and sugar are not restricted, while class II like benzoic acid, sulphites, and sorbic acid have concentration limits. They work by interfering with microbial cell membranes, enzymes, and genetics. Common chemical preservatives used are benzoic acid, sulphur dioxide, nitrates/nitrites, and sorbic acid. They are added after food processing and before packaging.
Food Packaging and materials .pptx
Food packaging has several key functions: protection, communication, convenience, and containment. It protects foods from damage and spoilage, provides information to consumers, increases ease of use and handling, and holds the food securely. Various materials are used for food packaging, including paper, paperboard, glass, metals, and plastics. Each material has advantages and disadvantages for different applications depending on its barrier properties and ability to preserve food quality during transport and storage.
Food Adulteration pptx
The document discusses food adulteration, including definitions, common adulterants, reasons for adulteration, and health effects. Some key points:
- Food adulteration is defined as adding substances to food that affect its composition or quality without the consumer's knowledge. Common adulterants include cheaper ingredients, toxic chemicals, and excessive water or preservatives.
- Adulteration is often done to increase profits by using lower quality ingredients, increase food volumes, or extend shelf life. It can have serious health consequences like cancer, organ damage, or death in some cases.
- Milk, ghee, spices and condiments are among the most commonly adulterated foods in India.
Biopreservation .pptx
This document discusses biopreservation techniques for extending the shelf life and safety of foods. It describes using beneficial microorganisms or their antimicrobial compounds to inhibit spoilage and pathogenic bacteria. Specific biopreservative agents discussed include lactic acid bacteria, yeasts, and bacteriophages. Lactic acid bacteria produce organic acids and bacteriocins that have antagonistic effects on other microbes. The document also examines applications of biopreservation in various food products and regulatory considerations for biopreservative agents.
YERSINIA .pptx
Yersinia is a genus of bacteria that includes three medically important species that can cause disease in humans and animals. Yersinia pestis specifically causes plague in humans and other mammals. It is a gram-negative, rod-shaped bacterium that was first discovered in 1894. Y. pestis can cause bubonic, pneumonic, or septicemic plague depending on how it enters the body. It is most commonly transmitted to humans via the bite of an infected flea that has acquired the bacteria from an infected rodent.
Vibrio cholera .pptx
Vibrio cholerae is a gram-negative, curved bacillus that causes the disease cholera. It was discovered independently by Filippo Pacini in 1854 in Italy and Robert Koch in 1883 in India. Cholera is typically spread through contaminated water and causes severe diarrhea and dehydration. Modern water treatment has eliminated cholera in most developed countries, but it remains problematic in parts of Asia, Africa, and South America where water treatment is lacking. Diagnosis involves examining stool samples under a microscope and culturing on selective media such as TCBS agar. Treatment focuses on oral rehydration therapy to replace lost fluids. Prevention relies on proper sanitation, boiling water, and oral cholera vaccines.
Vibrio Cholera .ppt
Vibrio cholerae is a gram-negative, curved rod-shaped bacterium that causes the disease cholera. It produces a cholera toxin that increases chloride secretion in intestinal cells, causing a massive outflow of watery diarrhea that can lead to dehydration, shock, and death if untreated. The disease is typically diagnosed by isolating V. cholerae from a patient's stool and identifying yellow, sucrose-fermenting colonies. Treatment involves prompt oral or intravenous rehydration to replace lost fluids, along with antibiotics to eliminate the bacteria. Proper sanitation and clean water supplies are critical for preventing cholera outbreaks.
Vaccines .pptx
This document discusses several types of vaccines including live attenuated vaccines, killed vaccines, toxoid vaccines, and recombinant vector vaccines. Live attenuated vaccines use weakened live pathogens to induce immunity, such as the BCG vaccine against tuberculosis and the oral polio vaccine. Killed vaccines use pathogens that have been grown and then killed to induce immunity without risk of infection, requiring booster doses. Toxoid vaccines use inactivated bacterial toxins, such as vaccines for tetanus and pertussis. Recombinant vector vaccines use recombinant DNA technology to produce antigens and induce immunity. DNA vaccines and peptide vaccines are also discussed as modern synthetic vaccine approaches.
TISSUE TYPING .pptx
Tissue typing is the process of determining compatibility between donor and recipient tissues by identifying their Human Leukocyte Antigen (HLA) types. HLA acts as a barcode to distinguish self from nonself. Tissue typing ensures a transplanted organ will be compatible with the recipient to reduce rejection. It is done by testing the donor and recipient's blood or tissue to identify their unique HLA antigens. Close matching of HLA antigens between donor and recipient increases the likelihood the recipient's body will accept the transplant. Molecular methods like sequence-based typing now allow highly accurate HLA typing.
SYSTEMIC MYCOSIS .pptx
Systemic mycoses are fungal infections that spread from the initial infection site via the bloodstream to multiple internal organs. They most commonly enter the body through the lungs, gut, or skin and can affect immunocompromised or otherwise healthy patients. Common symptoms include fever, cough, and loss of appetite. Diagnosis involves tissue biopsy and culture, while treatment requires prolonged courses of antifungal medications. Despite therapy, systemic mycoses often have poor outcomes.
Systemic lupus Erytromatosis and Graves’ Disease .pptx
This document discusses systemic lupus erythematosus (SLE) and Graves' disease. SLE is a chronic autoimmune disease that can affect the skin, joints, organs and tissues. It is more prevalent in women and certain ethnic groups. Symptoms range from mild to severe and can impact multiple body systems. Graves' disease is also an autoimmune disease where the immune system attacks the thyroid gland, causing it to produce excess thyroid hormones. This leads to hyperthyroidism with symptoms like eye bulging, rapid heart rate and weight loss. Both diseases have no known cures but can be treated and managed to relieve symptoms.
Subcutaneous mycoses K R.pptx
Sporotrichosis is a fungal infection caused by Sporothrix schenckii. It typically presents as firm, painless nodules on the skin that can spread and ulcerate. The fungus is commonly found in soil and plants, and infection usually occurs through skin trauma from these sources. Symptoms range from minimal to widespread depending on immune status. Treatment involves antifungal medications like itraconazole or potassium iodide for localized infection, and amphotericin B for more severe cases. Sporotrichosis can also affect animals like cats and is occasionally transmitted between animals and humans through skin contact.
SPIROCHAETES TREPONEMA K R .pptx
Spirochaetes are gram negative, elongated and motile bacteria with spiral shapes. Treponema pallidum causes syphilis in humans. It has a long incubation period and progresses through primary, secondary, latent and tertiary stages if left untreated. Primary syphilis presents as a chancre which disseminates systemically in secondary syphilis with rashes and mucous patches. Latent syphilis is asymptomatic but can affect the heart, brain or form gummata in tertiary syphilis. Diagnosis involves microscopy, serology and dark-field examination with treatment using penicillin.
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Preservation of Food and feed using irradiation .pptx
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Recently uploaded
Immersive Learning That Works: Research Grounding and Paths Forward
We will metaverse into the essence of immersive learning, into its three dimensions and conceptual models. This approach encompasses elements from teaching methodologies to social involvement, through organizational concerns and technologies. Challenging the perception of learning as knowledge transfer, we introduce a 'Uses, Practices & Strategies' model operationalized by the 'Immersive Learning Brain' and ‘Immersion Cube’ frameworks. This approach offers a comprehensive guide through the intricacies of immersive educational experiences and spotlighting research frontiers, along the immersion dimensions of system, narrative, and agency. Our discourse extends to stakeholders beyond the academic sphere, addressing the interests of technologists, instructional designers, and policymakers. We span various contexts, from formal education to organizational transformation to the new horizon of an AI-pervasive society. This keynote aims to unite the iLRN community in a collaborative journey towards a future where immersive learning research and practice coalesce, paving the way for innovative educational research and practice landscapes.
Applied Science: Thermodynamics, Laws & Methodology.pdf
When I was asked to give a companion lecture in support of ‘The Philosophy of Science’ (https://shorturl.at/4pUXz) I decided not to walk through the detail of the many methodologies in order of use. Instead, I chose to employ a long standing, and ongoing, scientific development as an exemplar. And so, I chose the ever evolving story of Thermodynamics as a scientific investigation at its best.
Conducted over a period of >200 years, Thermodynamics R&D, and application, benefitted from the highest levels of professionalism, collaboration, and technical thoroughness. New layers of application, methodology, and practice were made possible by the progressive advance of technology. In turn, this has seen measurement and modelling accuracy continually improved at a micro and macro level.
Perhaps most importantly, Thermodynamics rapidly became a primary tool in the advance of applied science/engineering/technology, spanning micro-tech, to aerospace and cosmology. I can think of no better a story to illustrate the breadth of scientific methodologies and applications at their best.
Describing and Interpreting an Immersive Learning Case with the Immersion Cub...
Current descriptions of immersive learning cases are often difficult or impossible to compare. This is due to a myriad of different options on what details to include, which aspects are relevant, and on the descriptive approaches employed. Also, these aspects often combine very specific details with more general guidelines or indicate intents and rationales without clarifying their implementation. In this paper we provide a method to describe immersive learning cases that is structured to enable comparisons, yet flexible enough to allow researchers and practitioners to decide which aspects to include. This method leverages a taxonomy that classifies educational aspects at three levels (uses, practices, and strategies) and then utilizes two frameworks, the Immersive Learning Brain and the Immersion Cube, to enable a structured description and interpretation of immersive learning cases. The method is then demonstrated on a published immersive learning case on training for wind turbine maintenance using virtual reality. Applying the method results in a structured artifact, the Immersive Learning Case Sheet, that tags the case with its proximal uses, practices, and strategies, and refines the free text case description to ensure that matching details are included. This contribution is thus a case description method in support of future comparative research of immersive learning cases. We then discuss how the resulting description and interpretation can be leveraged to change immersion learning cases, by enriching them (considering low-effort changes or additions) or innovating (exploring more challenging avenues of transformation). The method holds significant promise to support better-grounded research in immersive learning.
Pests of Storage_Identification_Dr.UPR.pdf
InIndia-post-harvestlosses-unscientificstorage,insects,rodents,micro-organismsetc.,accountforabout10percentoftotalfoodgrains
Graininfestation
Directdamage
Indirectly
•theexuviae,skin,deadinsects
•theirexcretawhichmakefoodunfitforhumanconsumption
About600speciesofinsectshavebeenassociatedwithstoredgrainproducts
100speciesofinsectpestsofstoredproductscauseeconomiclosses
Randomised Optimisation Algorithms in DAPHNE
Slides from talk:
Aleš Zamuda: Randomised Optimisation Algorithms in DAPHNE .
Austrian-Slovenian HPC Meeting 2024 – ASHPC24, Seeblickhotel Grundlsee in Austria, 10–13 June 2024
https://ashpc.eu/
8.Isolation of pure cultures and preservation of cultures.pdf
Isolation of pure culture, its various method.
EWOCS-I: The catalog of X-ray sources in Westerlund 1 from the Extended Weste...
Context. With a mass exceeding several 104 M⊙ and a rich and dense population of massive stars, supermassive young star clusters
represent the most massive star-forming environment that is dominated by the feedback from massive stars and gravitational interactions
among stars.
Aims. In this paper we present the Extended Westerlund 1 and 2 Open Clusters Survey (EWOCS) project, which aims to investigate
the influence of the starburst environment on the formation of stars and planets, and on the evolution of both low and high mass stars.
The primary targets of this project are Westerlund 1 and 2, the closest supermassive star clusters to the Sun.
Methods. The project is based primarily on recent observations conducted with the Chandra and JWST observatories. Specifically,
the Chandra survey of Westerlund 1 consists of 36 new ACIS-I observations, nearly co-pointed, for a total exposure time of 1 Msec.
Additionally, we included 8 archival Chandra/ACIS-S observations. This paper presents the resulting catalog of X-ray sources within
and around Westerlund 1. Sources were detected by combining various existing methods, and photon extraction and source validation
were carried out using the ACIS-Extract software.
Results. The EWOCS X-ray catalog comprises 5963 validated sources out of the 9420 initially provided to ACIS-Extract, reaching a
photon flux threshold of approximately 2 × 10−8 photons cm−2
s
−1
. The X-ray sources exhibit a highly concentrated spatial distribution,
with 1075 sources located within the central 1 arcmin. We have successfully detected X-ray emissions from 126 out of the 166 known
massive stars of the cluster, and we have collected over 71 000 photons from the magnetar CXO J164710.20-455217.
Equivariant neural networks and representation theory
Or: Beyond linear.
Abstract: Equivariant neural networks are neural networks that incorporate symmetries. The nonlinear activation functions in these networks result in interesting nonlinear equivariant maps between simple representations, and motivate the key player of this talk: piecewise linear representation theory.
Disclaimer: No one is perfect, so please mind that there might be mistakes and typos.
dtubbenhauer@gmail.com
Corrected slides: dtubbenhauer.com/talks.html
Direct Seeded Rice - Climate Smart Agriculture
Direct Seeded Rice - Climate Smart AgricultureInternational Food Policy Research Institute- South Asia Office
PPT on Direct Seeded Rice presented at the three-day 'Training and Validation Workshop on Modules of Climate Smart Agriculture (CSA) Technologies in South Asia' workshop on April 22, 2024.
The cost of acquiring information by natural selection
This is a short talk that I gave at the Banff International Research Station workshop on Modeling and Theory in Population Biology. The idea is to try to understand how the burden of natural selection relates to the amount of information that selection puts into the genome.
It's based on the first part of this research paper:
The cost of information acquisition by natural selection
Ryan Seamus McGee, Olivia Kosterlitz, Artem Kaznatcheev, Benjamin Kerr, Carl T. Bergstrom
bioRxiv 2022.07.02.498577; doi: https://doi.org/10.1101/2022.07.02.498577
SAR of Medicinal Chemistry 1st by dk.pdf
In this presentation include the prototype drug SAR on thus or with their examples .
Syllabus of Second Year B. Pharmacy
2019 PATTERN.
Compexometric titration/Chelatorphy titration/chelating titration
Classification
Metal ion ion indicators
Masking and demasking reagents
Estimation of Magnisium sulphate
Calcium gluconate
Complexometric Titration/ chelatometry titration/chelating titration, introduction, Types-
1.Direct Titration
2.Back Titration
3.Replacement Titration
4.Indirect Titration
Masking agent, Demasking agents
formation of complex
comparition between masking and demasking agents,
Indicators/Metal ion indicators/ Metallochromic indicators/pM indicators,
Visual Technique,PM indicators (metallochromic), Indicators of pH, Redox Indicators
Instrumental Techniques-Photometry
Potentiometry
Miscellaneous methods.
Complex titration with EDTA.
(June 12, 2024) Webinar: Development of PET theranostics targeting the molecu...
(June 12, 2024) Webinar: Development of PET theranostics targeting the molecu...Scintica Instrumentation
Targeting Hsp90 and its pathogen Orthologs with Tethered Inhibitors as a Diagnostic and Therapeutic Strategy for cancer and infectious diseases with Dr. Timothy Haystead.The debris of the ‘last major merger’ is dynamically young
The Milky Way’s (MW) inner stellar halo contains an [Fe/H]-rich component with highly eccentric orbits, often referred to as the
‘last major merger.’ Hypotheses for the origin of this component include Gaia-Sausage/Enceladus (GSE), where the progenitor
collided with the MW proto-disc 8–11 Gyr ago, and the Virgo Radial Merger (VRM), where the progenitor collided with the
MW disc within the last 3 Gyr. These two scenarios make different predictions about observable structure in local phase space,
because the morphology of debris depends on how long it has had to phase mix. The recently identified phase-space folds in Gaia
DR3 have positive caustic velocities, making them fundamentally different than the phase-mixed chevrons found in simulations
at late times. Roughly 20 per cent of the stars in the prograde local stellar halo are associated with the observed caustics. Based
on a simple phase-mixing model, the observed number of caustics are consistent with a merger that occurred 1–2 Gyr ago.
We also compare the observed phase-space distribution to FIRE-2 Latte simulations of GSE-like mergers, using a quantitative
measurement of phase mixing (2D causticality). The observed local phase-space distribution best matches the simulated data
1–2 Gyr after collision, and certainly not later than 3 Gyr. This is further evidence that the progenitor of the ‘last major merger’
did not collide with the MW proto-disc at early times, as is thought for the GSE, but instead collided with the MW disc within
the last few Gyr, consistent with the body of work surrounding the VRM.
Shallowest Oil Discovery of Turkiye.pptx
The Petroleum System of the Çukurova Field - the Shallowest Oil Discovery of Türkiye, Adana
THEMATIC APPERCEPTION TEST(TAT) cognitive abilities, creativity, and critic...
THEMATIC APPERCEPTION TEST(TAT) cognitive abilities, creativity, and critic...Abdul Wali Khan University Mardan,kP,Pakistan
hematic appreciation test is a psychological assessment tool used to measure an individual's appreciation and understanding of specific themes or topics. This test helps to evaluate an individual's ability to connect different ideas and concepts within a given theme, as well as their overall comprehension and interpretation skills. The results of the test can provide valuable insights into an individual's cognitive abilities, creativity, and critical thinking skillsThe binding of cosmological structures by massless topological defects
Assuming spherical symmetry and weak field, it is shown that if one solves the Poisson equation or the Einstein field
equations sourced by a topological defect, i.e. a singularity of a very specific form, the result is a localized gravitational
field capable of driving flat rotation (i.e. Keplerian circular orbits at a constant speed for all radii) of test masses on a thin
spherical shell without any underlying mass. Moreover, a large-scale structure which exploits this solution by assembling
concentrically a number of such topological defects can establish a flat stellar or galactic rotation curve, and can also deflect
light in the same manner as an equipotential (isothermal) sphere. Thus, the need for dark matter or modified gravity theory is
mitigated, at least in part.
在线办理(salfor毕业证书)索尔福德大学毕业证毕业完成信一模一样
学校原件一模一样【微信：741003700 】《(salfor毕业证书)索尔福德大学毕业证》【微信：741003700 】学位证，留信认证（真实可查，永久存档）原件一模一样纸张工艺/offer、雅思、外壳等材料/诚信可靠,可直接看成品样本，帮您解决无法毕业带来的各种难题！外壳，原版制作，诚信可靠，可直接看成品样本。行业标杆！精益求精，诚心合作，真诚制作！多年品质 ,按需精细制作，24小时接单,全套进口原装设备。十五年致力于帮助留学生解决难题，包您满意。
本公司拥有海外各大学样板无数，能完美还原。
1:1完美还原海外各大学毕业材料上的工艺：水印，阴影底纹，钢印LOGO烫金烫银，LOGO烫金烫银复合重叠。文字图案浮雕、激光镭射、紫外荧光、温感、复印防伪等防伪工艺。材料咨询办理、认证咨询办理请加学历顾问Q/微741003700
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二.真实使馆公证(即留学回国人员证明,不成功不收费)
三.真实教育部学历学位认证（教育部存档！教育部留服网站永久可查）
四.办理各国各大学文凭(一对一专业服务,可全程监控跟踪进度)
如果您处于以下几种情况：
◇在校期间，因各种原因未能顺利毕业……拿不到官方毕业证【q/微741003700】
◇面对父母的压力，希望尽快拿到；
◇不清楚认证流程以及材料该如何准备；
◇回国时间很长，忘记办理；
◇回国马上就要找工作，办给用人单位看；
◇企事业单位必须要求办理的
◇需要报考公务员、购买免税车、落转户口
◇申请留学生创业基金
留信网认证的作用:
1:该专业认证可证明留学生真实身份
2:同时对留学生所学专业登记给予评定
3:国家专业人才认证中心颁发入库证书
4:这个认证书并且可以归档倒地方
5:凡事获得留信网入网的信息将会逐步更新到个人身份内，将在公安局网内查询个人身份证信息后，同步读取人才网入库信息
6:个人职称评审加20分
7:个人信誉贷款加10分
8:在国家人才网主办的国家网络招聘大会中纳入资料，供国家高端企业选择人才
Recently uploaded (20)
Immersive Learning That Works: Research Grounding and Paths Forward
Immersive Learning That Works: Research Grounding and Paths Forward
Applied Science: Thermodynamics, Laws & Methodology.pdf
Applied Science: Thermodynamics, Laws & Methodology.pdf
Describing and Interpreting an Immersive Learning Case with the Immersion Cub...
Describing and Interpreting an Immersive Learning Case with the Immersion Cub...
8.Isolation of pure cultures and preservation of cultures.pdf
8.Isolation of pure cultures and preservation of cultures.pdf
EWOCS-I: The catalog of X-ray sources in Westerlund 1 from the Extended Weste...
EWOCS-I: The catalog of X-ray sources in Westerlund 1 from the Extended Weste...
Equivariant neural networks and representation theory
Equivariant neural networks and representation theory
The cost of acquiring information by natural selection
The cost of acquiring information by natural selection
Compexometric titration/Chelatorphy titration/chelating titration
Compexometric titration/Chelatorphy titration/chelating titration
(June 12, 2024) Webinar: Development of PET theranostics targeting the molecu...
(June 12, 2024) Webinar: Development of PET theranostics targeting the molecu...
The debris of the ‘last major merger’ is dynamically young
The debris of the ‘last major merger’ is dynamically young
THEMATIC APPERCEPTION TEST(TAT) cognitive abilities, creativity, and critic...
THEMATIC APPERCEPTION TEST(TAT) cognitive abilities, creativity, and critic...
The binding of cosmological structures by massless topological defects
The binding of cosmological structures by massless topological defects
Active sites-ENZYMES
- 1. --ACTIVE SITES --PROSTHETIC GROUP --FACTORS INFLUENCING ENZYME ACTIVITY
- 2. KKR1116 2
- 3. KKR1116 3
- 4. KKR1116 4
- 5. KKR1116 5
- 6. KKR1116 6
- 7. KKR1116 7
- 8. KKR1116 8
- 9. KKR1116 9
- 10. KKR1116 10
- 11. KKR1116 11
- 12. KKR1116 12
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- 14. PROSTHETIC GROUP A prosthetic group is the non-amino acid component that is part of the structure of the heteroproteins or conjugated proteins, being covalently linked to the apoprotein. This is a component of a conjugated protein that is required for the protein's biological activity. The prosthetic group may be organic (such as a vitamin, sugar, RNA, phosphate or lipid) or inorganic (such as a metal ion). Prosthetic groups are bound tightly to proteins and may even be attached through a covalent bond. They often play an important role in enzyme catalysis. KKR1116 14
- 15. A protein without its prosthetic group is called an apoprotein, while a protein combined with its prosthetic group is called a holoprotein. A non-covalently bound prosthetic group cannot generally be removed from the holoprotein without denaturating the protein. KKR1116 15
- 17. FACTORS INFLUENCING ENZYME ACTIVITY 1. TEMPERATURE 2. pH 3. CONCENTRATION OF ENZYME 4. CONCENTRATION OF SUBSTRATE KKR1116 17
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- 28. REFERENCE WWW.WIKEPEDIA.COM MICROBIOLOGY BY MICHAEL.J.PELCZAR Jr SHOMU’S BIOLOGY MICROBENOTES.COM KKR1116 28
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