1. General Structure of Amino Acids
2. Amino acids classification based on:
- Standard and Non-standard amino acids (AA)
- Essential and non-essential AA
- Ketogenic and Glycogenic AA
- Side chain functional group
3. Function of essential Amino Acids
The document discusses the structure and classification of amino acids. It covers the general structure of amino acids including their carboxyl and amino groups. Amino acids are classified based on whether they are standard or non-standard, essential or non-essential, ketogenic or glucogenic, and their side chain groups. Essential amino acids play important roles in processes like neurotransmitter synthesis, hormone production, and serving as precursors for other amino acids.
1. The document discusses the chemistry of amino acids, which are the building blocks of proteins. It defines amino acids and their basic structure, and classifies them as standard and non-standard amino acids.
2. Amino acids are classified based on the nature of their side chains as hydrophobic, hydrophilic, positively charged, or negatively charged. Their side chains determine their properties and allow some amino acids to perform specific roles in proteins.
3. The document also discusses the essential, non-essential, and semi-essential amino acids based on nutritional requirements, and classifies amino acids as glucogenic, ketogenic, or both based on their metabolic fate.
This presentation the chemical structure of natural amino acids. It also classifies amino acids according to several criteria e.g., structure (aliphatic, aromatic, and heterocyclic amino acids), reaction (Neutral, acidic and basic amino acids), polarity (polar and nonpolar amino acids), and metabolic fate ( glucogenic, ketogenic and glucoketogenic amino acids)
General structure of amino acid
Specific learning objective (SLO): Amino acid as Ampholytes (acid and base), Zwitter ions.
Classification of amino acid on the basis of side chain, chemical composition, Nutritional Requirement and metabolic fate.
Derived amino acids.
Optical properties of amino acids.
Acid-Base properties and Buffer characteristic.
Biological Important Peptides
Proteins based on nutritional value
Lec2 amino.a.classification microsoft powerDrShamimAkram
Ā
Amino acids can be classified in several ways:
1. Based on their source as either standard/primary amino acids that are incorporated into proteins or non-standard amino acids that do not participate in protein synthesis.
2. By the properties of their side chains as non-polar, polar uncharged, acidic, or basic. Non-polar amino acids cluster inside proteins while polar ones interact through hydrogen bonding.
3. According to their roles in metabolism as either glycogenic, ketogenic, or both glycogenic and ketogenic.
Selenocysteine, containing the element selenium, is now recognized as the 21st standard amino acid despite being incorporated via a unique genetic mechanism during translation.
1) Amino acids can be classified based on their source, side chain structure, amphoteric properties, nutritional requirements, and metabolic fate. 2) The 20 standard amino acids are incorporated into proteins during translation based on codon sequences, while non-standard amino acids play other important biological roles. 3) Selenocysteine is the 21st amino acid encoded by UGA codons when accompanied by a selenocysteine insertion sequence in mRNA.
Some reagents or conditions that can cause protein denaturation include:
- High or low pH (acids and bases)
- Heat
- Detergents
- Organic solvents (alcohol, acetone)
- Heavy metals (salts of heavy metals like copper, mercury)
- Radiation (UV light, X-rays)
This document provides information on proteins and amino acids. It discusses that proteins are the most abundant organic molecules in living systems and are composed of amino acids. It then describes the 20 standard amino acids, how they are classified based on structure and properties. The document also discusses the nutritional classification of amino acids as essential or non-essential and their metabolic roles as being glucogenic, ketogenic or both.
The document discusses the structure and classification of amino acids. It covers the general structure of amino acids including their carboxyl and amino groups. Amino acids are classified based on whether they are standard or non-standard, essential or non-essential, ketogenic or glucogenic, and their side chain groups. Essential amino acids play important roles in processes like neurotransmitter synthesis, hormone production, and serving as precursors for other amino acids.
1. The document discusses the chemistry of amino acids, which are the building blocks of proteins. It defines amino acids and their basic structure, and classifies them as standard and non-standard amino acids.
2. Amino acids are classified based on the nature of their side chains as hydrophobic, hydrophilic, positively charged, or negatively charged. Their side chains determine their properties and allow some amino acids to perform specific roles in proteins.
3. The document also discusses the essential, non-essential, and semi-essential amino acids based on nutritional requirements, and classifies amino acids as glucogenic, ketogenic, or both based on their metabolic fate.
This presentation the chemical structure of natural amino acids. It also classifies amino acids according to several criteria e.g., structure (aliphatic, aromatic, and heterocyclic amino acids), reaction (Neutral, acidic and basic amino acids), polarity (polar and nonpolar amino acids), and metabolic fate ( glucogenic, ketogenic and glucoketogenic amino acids)
General structure of amino acid
Specific learning objective (SLO): Amino acid as Ampholytes (acid and base), Zwitter ions.
Classification of amino acid on the basis of side chain, chemical composition, Nutritional Requirement and metabolic fate.
Derived amino acids.
Optical properties of amino acids.
Acid-Base properties and Buffer characteristic.
Biological Important Peptides
Proteins based on nutritional value
Lec2 amino.a.classification microsoft powerDrShamimAkram
Ā
Amino acids can be classified in several ways:
1. Based on their source as either standard/primary amino acids that are incorporated into proteins or non-standard amino acids that do not participate in protein synthesis.
2. By the properties of their side chains as non-polar, polar uncharged, acidic, or basic. Non-polar amino acids cluster inside proteins while polar ones interact through hydrogen bonding.
3. According to their roles in metabolism as either glycogenic, ketogenic, or both glycogenic and ketogenic.
Selenocysteine, containing the element selenium, is now recognized as the 21st standard amino acid despite being incorporated via a unique genetic mechanism during translation.
1) Amino acids can be classified based on their source, side chain structure, amphoteric properties, nutritional requirements, and metabolic fate. 2) The 20 standard amino acids are incorporated into proteins during translation based on codon sequences, while non-standard amino acids play other important biological roles. 3) Selenocysteine is the 21st amino acid encoded by UGA codons when accompanied by a selenocysteine insertion sequence in mRNA.
Some reagents or conditions that can cause protein denaturation include:
- High or low pH (acids and bases)
- Heat
- Detergents
- Organic solvents (alcohol, acetone)
- Heavy metals (salts of heavy metals like copper, mercury)
- Radiation (UV light, X-rays)
This document provides information on proteins and amino acids. It discusses that proteins are the most abundant organic molecules in living systems and are composed of amino acids. It then describes the 20 standard amino acids, how they are classified based on structure and properties. The document also discusses the nutritional classification of amino acids as essential or non-essential and their metabolic roles as being glucogenic, ketogenic or both.
Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up proteins. Amino acids have a general structure that includes an amino group, a carboxyl group, and a side chain. They can be classified based on their structure, side chain properties, nutritional requirements, and metabolic fate. Common properties of amino acids include being crystalline solids, existing as zwitterions with an isoelectric point, and having chirality with L and D isomers. Amino acids undergo various reactions due to their amino, carboxyl, and side chain groups.
This document discusses amino acids, which are the building blocks of proteins. It defines amino acids and their basic structure, which includes an amino group, carboxyl group, and side chain. The document then classifies amino acids according to their side chains and discusses their optical, acid-base, and buffer properties. It also distinguishes between standard and non-standard amino acids, and essential vs non-essential amino acids which must be obtained through diet.
Amino acids are the building blocks of proteins. There are about 300 amino acids that occur in nature, but only 20 are used to build proteins. Each amino acid contains an amino group, a carboxyl group, a hydrogen atom, and a side chain that gives each amino acid its unique properties. At physiological pH, amino acids exist as zwitterions with both a positive and negative charge. The order and types of amino acids linked together determines a protein's structure and function. Amino acids can be classified based on their structure, side chain properties, nutritional needs, and metabolic fate.
There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves hydrogen bonding between amino acids to form common structures like alpha helices and beta sheets. Tertiary structure describes the three-dimensional folding of the protein chain stabilized by interactions between R groups. Quaternary structure refers to complexes of multiple polypeptide subunits. Proteins are classified based on their structure, composition, and function. Fibrous, globular, and intermediate proteins are distinguished by their structure, while simple and conjugated proteins differ in whether they contain additional non-protein groups.
This document discusses the chemistry of proteins. It begins by classifying proteins and their functions in organisms. It then discusses the structure and properties of amino acids, including their classification based on structure, polarity, nutrition requirements, and metabolic fate. It introduces peptides and peptide bonds. Key points are that proteins are composed of amino acids joined by peptide bonds, there are 20 standard amino acids, and proteins serve important structural and dynamic roles in organisms.
This document discusses amino acids, which are the building blocks of proteins. It covers the general structure of amino acids and various ways of classifying them, including as standard or non-standard, essential or non-essential, and based on their side chain functional groups and metabolic properties. The document also explains that proteins are synthesized from 20 common amino acids specified by the genetic code, and describes some key functions of essential amino acids like phenylalanine and tryptophan.
The document discusses amino acids, the building blocks of proteins. It describes the basic structure of an amino acid, which consists of a central carbon atom bonded to an amino group, carboxyl group, hydrogen atom, and variable R group. The 20 standard amino acids that make up proteins are specified. The amino acids are classified based on properties of their R groups, including polarity and charge. The document also discusses how amino acids join together via peptide bonds to form polypeptides and proteins, and the four levels of protein structure that determine a protein's function.
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They perform important functions including serving as monomers for protein synthesis, participating in cellular processes, and acting as precursors for other compounds.
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They have physical properties like solubility and melting points. Amino acids play important roles in many biological functions and reactions due to their amino, carboxyl, and side chain groups. They are essential for protein synthesis, cellular functions, and as precursors for other biomolecules.
Proteins are polymers of amino acids and perform a variety of essential functions in living cells. They can be classified based on their structure, composition, and properties. The main types are globular and fibrous proteins. Globular proteins are spherical and soluble, while fibrous proteins are elongated and form connections between tissues. Proteins are also classified as simple proteins containing only amino acids, or conjugated proteins which contain non-amino acid groups like carbohydrates, lipids, or metals. Amino acids polymerize to form peptide bonds, linking them into protein chains.
This document discusses amino acids, which are the building blocks of proteins. It defines amino acids as molecules containing both carboxyl and amine groups. There are over 300 amino acids found in nature, but only 22 are used as the standard building blocks in proteins. These standard amino acids differ in the side chain (R group) attached to their alpha carbon. Amino acids join together via peptide bonds to form protein chains. Proteins are essential to all living organisms and are formed through the process of translation.
Biomolecules are organic compounds that are present in living organisms. The four primary types of biomolecules are carbohydrates, lipids, proteins, and nucleic acids. Carbon is the most important element in biomolecules as it can form diverse and complex organic compounds through its ability to form bonds with four other atoms. Proteins are polymers of amino acids, while nucleic acids are polymers of nucleotides. Amino acids and nucleotides are the basic monomeric units that join together through condensation reactions to form the larger macromolecules. There are 20 standard amino acids that make up proteins in living organisms.
Here are the key points from the protein separation methods reading:
- There are several methods used to separate proteins including precipitation, electrophoresis, chromatography, and ultracentrifugation.
- Precipitation separates proteins based on differences in solubility at various pH, temperatures, or in the presence of salts, organic solvents, or other reagents. It is a crude separation method.
- Electrophoresis separates proteins based on their charge and size by applying an electric current through a gel or liquid. Common types are PAGE and SDS-PAGE.
- Chromatography separates proteins based on differences in how they interact with a stationary phase compared to a mobile phase as they flow through a column. Key types are ion-exchange
- Amino acids are the building blocks of proteins. They contain an amino group, a carboxyl group, an alpha carbon and different side chains attached to the alpha carbon.
- At physiological pH, amino acids exist as zwitterions with both positive and negative charges. There are 20 common amino acids that make up proteins. The order and structure of amino acids determines the structure and function of proteins.
- Amino acids can be classified based on their structure, side chains, nutritional requirements and metabolic fate. Many amino acids are essential and must be obtained through diet. Amino acids play important roles in human health and disease.
Amino acids are organic compounds that contain an amino group and a carboxyl group. There are over 300 amino acids found in nature, but only 20 are used as building blocks of proteins in the body. Each amino acid contains an alpha carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and a unique side chain. At physiological pH, amino acids exist as zwitterions with both positive and negative charges. Amino acids join together via peptide bonds to form polypeptides and proteins. The 20 standard amino acids are classified based on properties like polarity and acidity of their side chains. Amino acids and proteins are essential for building body tissues and important biomolecules like enzymes, hormones
This was a report regarding amino acids and peptides that was prepared by our group and this report made in order to make a score. Hope this slide makes more it to be on help.
There are 20 amino acids that are the building blocks of proteins. Amino acids are classified based on their polarity and the nature of their side chains. They can be hydrophobic, hydrophilic neutral, acidic, or basic. Proteins are polymers of amino acids joined by peptide bonds. They have primary, secondary, tertiary, and quaternary levels of structure that determine their shape and function. Denaturation disrupts a protein's structure leading to loss of biological activity.
Amino acids are the building blocks of proteins. They contain an amino group, a carboxyl group, and a side chain. There are 22 protein amino acids that are polymerized to form proteins, which carry out important structural and functional roles in the body. Amino acids can also be classified based on their chemical properties and metabolic fates. The peptide bond forms when amino acids condense, linking them together into polypeptides and proteins.
Describe factors affecting nitrogen balance in health and disease
š ¶ Explain rationale of urea cycle in ammonia excretion
š ¶ List two subcellular compartments used by urea cycle
š ¶ Describe reactions of Urea Cycle, including specific enzymes, input substrates (NH4, HCO3, ornithine, and aspartate), and energy requirements
š ¶ Describe urea cycle regulation by allosteric effectors, substrate availability, and
enzyme levels
š ¶ Outline steps of Urea cycle and inherited disorders associated with urea cycle
š ¶ Identify connections and common intermediates between Urea Cycle and TCA cycle
Formation & Transport of Ammonia and its Associated DisordersRahul SIR
Ā
Outline formation and transport of ammonia
š ¶ Describe importance of reactions catalyzed by glutamine synthetase, glutaminase, and glutamate dehydrogenase
š ¶ Role of Glutamine in Nitrogen metabolism
š ¶ Ammonia Intoxication
š ¶ List causes for hyperammonemia, its consequences, and treatments to reduce blood ammonia levels.
Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up proteins. Amino acids have a general structure that includes an amino group, a carboxyl group, and a side chain. They can be classified based on their structure, side chain properties, nutritional requirements, and metabolic fate. Common properties of amino acids include being crystalline solids, existing as zwitterions with an isoelectric point, and having chirality with L and D isomers. Amino acids undergo various reactions due to their amino, carboxyl, and side chain groups.
This document discusses amino acids, which are the building blocks of proteins. It defines amino acids and their basic structure, which includes an amino group, carboxyl group, and side chain. The document then classifies amino acids according to their side chains and discusses their optical, acid-base, and buffer properties. It also distinguishes between standard and non-standard amino acids, and essential vs non-essential amino acids which must be obtained through diet.
Amino acids are the building blocks of proteins. There are about 300 amino acids that occur in nature, but only 20 are used to build proteins. Each amino acid contains an amino group, a carboxyl group, a hydrogen atom, and a side chain that gives each amino acid its unique properties. At physiological pH, amino acids exist as zwitterions with both a positive and negative charge. The order and types of amino acids linked together determines a protein's structure and function. Amino acids can be classified based on their structure, side chain properties, nutritional needs, and metabolic fate.
There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves hydrogen bonding between amino acids to form common structures like alpha helices and beta sheets. Tertiary structure describes the three-dimensional folding of the protein chain stabilized by interactions between R groups. Quaternary structure refers to complexes of multiple polypeptide subunits. Proteins are classified based on their structure, composition, and function. Fibrous, globular, and intermediate proteins are distinguished by their structure, while simple and conjugated proteins differ in whether they contain additional non-protein groups.
This document discusses the chemistry of proteins. It begins by classifying proteins and their functions in organisms. It then discusses the structure and properties of amino acids, including their classification based on structure, polarity, nutrition requirements, and metabolic fate. It introduces peptides and peptide bonds. Key points are that proteins are composed of amino acids joined by peptide bonds, there are 20 standard amino acids, and proteins serve important structural and dynamic roles in organisms.
This document discusses amino acids, which are the building blocks of proteins. It covers the general structure of amino acids and various ways of classifying them, including as standard or non-standard, essential or non-essential, and based on their side chain functional groups and metabolic properties. The document also explains that proteins are synthesized from 20 common amino acids specified by the genetic code, and describes some key functions of essential amino acids like phenylalanine and tryptophan.
The document discusses amino acids, the building blocks of proteins. It describes the basic structure of an amino acid, which consists of a central carbon atom bonded to an amino group, carboxyl group, hydrogen atom, and variable R group. The 20 standard amino acids that make up proteins are specified. The amino acids are classified based on properties of their R groups, including polarity and charge. The document also discusses how amino acids join together via peptide bonds to form polypeptides and proteins, and the four levels of protein structure that determine a protein's function.
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They perform important functions including serving as monomers for protein synthesis, participating in cellular processes, and acting as precursors for other compounds.
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They have physical properties like solubility and melting points. Amino acids play important roles in many biological functions and reactions due to their amino, carboxyl, and side chain groups. They are essential for protein synthesis, cellular functions, and as precursors for other biomolecules.
Proteins are polymers of amino acids and perform a variety of essential functions in living cells. They can be classified based on their structure, composition, and properties. The main types are globular and fibrous proteins. Globular proteins are spherical and soluble, while fibrous proteins are elongated and form connections between tissues. Proteins are also classified as simple proteins containing only amino acids, or conjugated proteins which contain non-amino acid groups like carbohydrates, lipids, or metals. Amino acids polymerize to form peptide bonds, linking them into protein chains.
This document discusses amino acids, which are the building blocks of proteins. It defines amino acids as molecules containing both carboxyl and amine groups. There are over 300 amino acids found in nature, but only 22 are used as the standard building blocks in proteins. These standard amino acids differ in the side chain (R group) attached to their alpha carbon. Amino acids join together via peptide bonds to form protein chains. Proteins are essential to all living organisms and are formed through the process of translation.
Biomolecules are organic compounds that are present in living organisms. The four primary types of biomolecules are carbohydrates, lipids, proteins, and nucleic acids. Carbon is the most important element in biomolecules as it can form diverse and complex organic compounds through its ability to form bonds with four other atoms. Proteins are polymers of amino acids, while nucleic acids are polymers of nucleotides. Amino acids and nucleotides are the basic monomeric units that join together through condensation reactions to form the larger macromolecules. There are 20 standard amino acids that make up proteins in living organisms.
Here are the key points from the protein separation methods reading:
- There are several methods used to separate proteins including precipitation, electrophoresis, chromatography, and ultracentrifugation.
- Precipitation separates proteins based on differences in solubility at various pH, temperatures, or in the presence of salts, organic solvents, or other reagents. It is a crude separation method.
- Electrophoresis separates proteins based on their charge and size by applying an electric current through a gel or liquid. Common types are PAGE and SDS-PAGE.
- Chromatography separates proteins based on differences in how they interact with a stationary phase compared to a mobile phase as they flow through a column. Key types are ion-exchange
- Amino acids are the building blocks of proteins. They contain an amino group, a carboxyl group, an alpha carbon and different side chains attached to the alpha carbon.
- At physiological pH, amino acids exist as zwitterions with both positive and negative charges. There are 20 common amino acids that make up proteins. The order and structure of amino acids determines the structure and function of proteins.
- Amino acids can be classified based on their structure, side chains, nutritional requirements and metabolic fate. Many amino acids are essential and must be obtained through diet. Amino acids play important roles in human health and disease.
Amino acids are organic compounds that contain an amino group and a carboxyl group. There are over 300 amino acids found in nature, but only 20 are used as building blocks of proteins in the body. Each amino acid contains an alpha carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and a unique side chain. At physiological pH, amino acids exist as zwitterions with both positive and negative charges. Amino acids join together via peptide bonds to form polypeptides and proteins. The 20 standard amino acids are classified based on properties like polarity and acidity of their side chains. Amino acids and proteins are essential for building body tissues and important biomolecules like enzymes, hormones
This was a report regarding amino acids and peptides that was prepared by our group and this report made in order to make a score. Hope this slide makes more it to be on help.
There are 20 amino acids that are the building blocks of proteins. Amino acids are classified based on their polarity and the nature of their side chains. They can be hydrophobic, hydrophilic neutral, acidic, or basic. Proteins are polymers of amino acids joined by peptide bonds. They have primary, secondary, tertiary, and quaternary levels of structure that determine their shape and function. Denaturation disrupts a protein's structure leading to loss of biological activity.
Amino acids are the building blocks of proteins. They contain an amino group, a carboxyl group, and a side chain. There are 22 protein amino acids that are polymerized to form proteins, which carry out important structural and functional roles in the body. Amino acids can also be classified based on their chemical properties and metabolic fates. The peptide bond forms when amino acids condense, linking them together into polypeptides and proteins.
Describe factors affecting nitrogen balance in health and disease
š ¶ Explain rationale of urea cycle in ammonia excretion
š ¶ List two subcellular compartments used by urea cycle
š ¶ Describe reactions of Urea Cycle, including specific enzymes, input substrates (NH4, HCO3, ornithine, and aspartate), and energy requirements
š ¶ Describe urea cycle regulation by allosteric effectors, substrate availability, and
enzyme levels
š ¶ Outline steps of Urea cycle and inherited disorders associated with urea cycle
š ¶ Identify connections and common intermediates between Urea Cycle and TCA cycle
Formation & Transport of Ammonia and its Associated DisordersRahul SIR
Ā
Outline formation and transport of ammonia
š ¶ Describe importance of reactions catalyzed by glutamine synthetase, glutaminase, and glutamate dehydrogenase
š ¶ Role of Glutamine in Nitrogen metabolism
š ¶ Ammonia Intoxication
š ¶ List causes for hyperammonemia, its consequences, and treatments to reduce blood ammonia levels.
Fates of Amino Acids
š ¶ Amino Acid Utilization
š ¶ Amino-group metabolism
š ¶ Explain role of transamination reactions in aa synthesis and identify vitamin essential for this reaction (tie in to urea cycle)
š ¶ Describe interconversion between ketoacids and AA, including requirement of
pyridoxal phosphate (PLP) as a cofactor
š ¶ Outline formation and transport of ammonia
š ¶ Describe importance of reactions catalyzed by glutamine synthetase, glutaminase, and glutamate dehydrogenase
š ¶ Ammonia Intoxication
š ¶List causes for hyperammonemia, its consequences, and treatments to reduce blood ammonia levels
Properties of amino acids:
- Amino Acids have an Asymmetric Center
- D and L stereoisomerism of amino acids
- Acid-Base Properties of Amino Acids
- Titration of amino acids
- Absorption
- Solubility
- Chemical properties of amino acid
Ingestion, Digestion & Absorption of Dietary Proteins.pptxRahul SIR
Ā
Rahul is a lecturer in the Department of Med-Surg and co-chair of the South East Asia Regional Hub within the Challenger's Committee at Nursing Now Challenge in London. He has experience in biochemistry. The document expresses gratitude with a smiley face emoji.
Rahul is a lecturer in the Department of Med-Surg and also serves as the Zonal Vice-president at Nursing Teacherās Association of India in Ayodhya. Additionally, he is the Co-chair of the South East Asia Regional Hub within the Challengerās Committee for the Nursing Now Challenge based in London, UK.
The oral cavity includes the following:
1. The front two thirds of the tongue
2. The gingiva (gums)
3. The buccal mucosa (the lining of the inside of the cheeks)
4. The floor (bottom) of the mouth under the tongue
5. The hard palate (the roof of the mouth)
6. The retromolar trigone (the small area behind the wisdom teeth)
Oral cancer, also called mouth cancer, forms in the oral cavity, which includes all parts of your mouth that you can see if you open wide and look in the mirror. Your lips, gums, tongue, cheeks, roof or floor of the mouth. Oral cancer forms when cells on the lips or in the mouth mutate.
A speech disorder is a condition in which a person has problems creating or forming the speech sounds needed to communicate with others. This can make the child's speech difficult to understand.
Common speech disorders are:
1. Articulation disorders
2. Phonological disorders
3. Disfluency
4. Voice disorders or resonance disorders
The skeletal system consists of 206 bones that are divided into the axial skeleton (skull, vertebral column, ribs, sternum) and appendicular skeleton (limbs and their attaching girdles). Bones provide structure, protection, movement, mineral storage, blood cell formation, and are living tissues that undergo remodeling. The skeletal system includes various bone cell types and bone is composed of inorganic minerals and organic matrix. Common diseases include osteoporosis, rickets, osteomalacia, and Paget's disease.
Airway Suctioning
OUTLINES:
1- Definition of suctioning .
2- Sites for suction .
3- Deferent between oropharyngeal / nasopharyngeal suctioning and endotracheal / tracheostomy suctioning .
4- Purposes for suctioning .
5- Indications for suctioning.
6- Choosing the right size catheter.
7- Setting the correct pressure .
8- The procedure .
9- Documentation.
10- Complications of suctioning .
11- Techniques to minimize or decrease the complications .
Exploiting Artificial Intelligence for Empowering Researchers and Faculty, In...Dr. Vinod Kumar Kanvaria
Ā
Exploiting Artificial Intelligence for Empowering Researchers and Faculty,
International FDP on Fundamentals of Research in Social Sciences
at Integral University, Lucknow, 06.06.2024
By Dr. Vinod Kumar Kanvaria
This slide is special for master students (MIBS & MIFB) in UUM. Also useful for readers who are interested in the topic of contemporary Islamic banking.
Main Java[All of the Base Concepts}.docxadhitya5119
Ā
This is part 1 of my Java Learning Journey. This Contains Custom methods, classes, constructors, packages, multithreading , try- catch block, finally block and more.
A review of the growth of the Israel Genealogy Research Association Database Collection for the last 12 months. Our collection is now passed the 3 million mark and still growing. See which archives have contributed the most. See the different types of records we have, and which years have had records added. You can also see what we have for the future.
How to Build a Module in Odoo 17 Using the Scaffold MethodCeline George
Ā
Odoo provides an option for creating a module by using a single line command. By using this command the user can make a whole structure of a module. It is very easy for a beginner to make a module. There is no need to make each file manually. This slide will show how to create a module using the scaffold method.
Macroeconomics- Movie Location
This will be used as part of your Personal Professional Portfolio once graded.
Objective:
Prepare a presentation or a paper using research, basic comparative analysis, data organization and application of economic information. You will make an informed assessment of an economic climate outside of the United States to accomplish an entertainment industry objective.
Introduction to AI for Nonprofits with Tapp NetworkTechSoup
Ā
Dive into the world of AI! Experts Jon Hill and Tareq Monaur will guide you through AI's role in enhancing nonprofit websites and basic marketing strategies, making it easy to understand and apply.
June 3, 2024 Anti-Semitism Letter Sent to MIT President Kornbluth and MIT Cor...Levi Shapiro
Ā
Letter from the Congress of the United States regarding Anti-Semitism sent June 3rd to MIT President Sally Kornbluth, MIT Corp Chair, Mark Gorenberg
Dear Dr. Kornbluth and Mr. Gorenberg,
The US House of Representatives is deeply concerned by ongoing and pervasive acts of antisemitic
harassment and intimidation at the Massachusetts Institute of Technology (MIT). Failing to act decisively to ensure a safe learning environment for all students would be a grave dereliction of your responsibilities as President of MIT and Chair of the MIT Corporation.
This Congress will not stand idly by and allow an environment hostile to Jewish students to persist. The House believes that your institution is in violation of Title VI of the Civil Rights Act, and the inability or
unwillingness to rectify this violation through action requires accountability.
Postsecondary education is a unique opportunity for students to learn and have their ideas and beliefs challenged. However, universities receiving hundreds of millions of federal funds annually have denied
students that opportunity and have been hijacked to become venues for the promotion of terrorism, antisemitic harassment and intimidation, unlawful encampments, and in some cases, assaults and riots.
The House of Representatives will not countenance the use of federal funds to indoctrinate students into hateful, antisemitic, anti-American supporters of terrorism. Investigations into campus antisemitism by the Committee on Education and the Workforce and the Committee on Ways and Means have been expanded into a Congress-wide probe across all relevant jurisdictions to address this national crisis. The undersigned Committees will conduct oversight into the use of federal funds at MIT and its learning environment under authorities granted to each Committee.
ā¢ The Committee on Education and the Workforce has been investigating your institution since December 7, 2023. The Committee has broad jurisdiction over postsecondary education, including its compliance with Title VI of the Civil Rights Act, campus safety concerns over disruptions to the learning environment, and the awarding of federal student aid under the Higher Education Act.
ā¢ The Committee on Oversight and Accountability is investigating the sources of funding and other support flowing to groups espousing pro-Hamas propaganda and engaged in antisemitic harassment and intimidation of students. The Committee on Oversight and Accountability is the principal oversight committee of the US House of Representatives and has broad authority to investigate āany matterā at āany timeā under House Rule X.
ā¢ The Committee on Ways and Means has been investigating several universities since November 15, 2023, when the Committee held a hearing entitled From Ivory Towers to Dark Corners: Investigating the Nexus Between Antisemitism, Tax-Exempt Universities, and Terror Financing. The Committee followed the hearing with letters to those institutions on January 10, 202
1. Bio-Chemistry
Rahul SIR
Lecturer, Department of Med-Surg
Co-chair of the South East Asia Regional Hub within the
Challengerās Committee at Nursing Now Challenge, London, UK
āStructures of Amino Acidsā
2. Specific Learning Objectives
1. General Structure of amino acids
2. Amino acids classification based on:
ā¢Standard and Non-standard amino acids (aa)
ā¢Essential and non-essential aa
ā¢Ketogenic and Glucogenic aa
ā¢Side chain functional group
3. Function of essential amino acids
3. Introduction
ā¢Amino acids as a building blocks of peptides and proteins
ā¢Proteins are made up of hundreds of smaller units called amino acids that are
attached to one another by peptide bonds, forming a long chain.
ā¢Protein as a string of beads where each bead is an amino acid.
www.khanacademy.org
4. Genetic Code Specifies 20 L-Ī±-Amino Acids
ā¢Proteins are synthesized from the set of 20 L-Ī±-amino acids encoded by nucleotide
triplets called codons.
ā¢Common amino acids are those for which at least one specific codon exists in
the DNA genetic code.
ā¢Sequences of peptides and proteins represent by using one- and three letter
abbreviations for each amino acid.
5. Genetic information is transcribed from a DNA sequence into mRNA
and then translated to amino acid sequence of a protein
Fig. 2.1. Textbook of Biochemistry with Clinical Correlations, 4th edition by Thomas M Devlin
6. General Structure of Common Amino Acids
ā¢General structure of amino acids , group and a variable side chain
ā¢Side chain determines: protein folding, binding to specific ligand and interaction
with its environment
ā¢Amino acids consists of a constant COOH (R is side chain)
ā¢At neutral pH, H2N- protonated to H3N+-, and āCOOH deprotonated to āCOO-
Fig.4.2.Biochemistry. 4th edition by Donald Voet and Judith G. Voet
7. Amino-Acids Classification Based on Standard and Non-
Standard Amino Acids
1. Standard amino-acids: Those 20 amino acids are encoded by universal
genetic code
2. Non-Standard amino-acids: Two amino acids incorporated into proteins by
unique synthetic mechanism
ā¢Selenocysteine: Incorporated when mRNA translated included SECIS
(selenocysteine insertion seq) element, causes the UGA codon to encode
selenocysteine instead of stop codon)
ā¢Pyrrolysine: used by methanogenic archaea in enzyme that they use to produce
methane. It is coded for UAG stop codon.
8. Standard amino acids
ā¢All proteins are composed of the 20 āstandard "amino acids.
ā¢Common central alpha (Ī±)-carbon atom bound to a carboxylic acid group, an
amino group and a hydrogen atom are covalently bonded.
ā¢They have a primary amino group and a carboxylic acid group substituent on the
same carbon atom, with the exception of proline, (has a secondary amino group).
Fig.4.1. Biochemistry. 4th edition by Donald Voet and Judith G. Voet
9. How Proline gives conformational rigidity?
ā¢Proline classified as an imino acid, its Ī±-amine is a secondary amine with its a
nitrogen having two covalent bonds to carbon (to the Ī±-carbon and side chain
carbon), rather than primary amine
ā¢Incorporation of amino nitrogen into a five membered ring constrains rotational
freedom around āNĪ±-CĪ±-bond in proline to specific rotational angle, reduces
structural flexibility of polypeptide regions containing proline.
Ī±
10. Non-Standard Amino Acids
ā¢Selenocysteine, 21st protein L-Ī± amino acids
ā¢Selenium atom replaces the sulfur of its elemental analog, cysteine
ā¢Selenocysteine is not the product of a posttranslational modification, but is inserted
directly into a growing polypeptide during translation.
ā¢Selenocysteine is charged on a special tRNA called tRNASec specific for UGA
(STOP)codon inserted into growing polypeptide during translation
11. Other Classification of Amino Acids
ā¢Non-protein aa: Not naturally encoded by genetic code but found in free state as
intermediates of metabolic pathway for standard aa: Ornithine and citrulline are
intermediates in urea biosynthesis.
ā¢ Non Ī±-aa: -NH2 group not attached to Ī±-carbon atom but some other carbon
atom. Ex. Ī³-aminobutyric acid (GABA) and Ī²-alanine.
ā¢Modified protein aa: Amino acids modified after they incorporated into protein.
Proline and lysine undergo hydroxylation to become hydroxyproline and
Hydroxylysine. Essential for formation of mature collagen.
12. AA Classified on Basis of Nutritional Requirement
ā¢Essential amino acids: Not synthesised in the body and must be supplied in diet
ā¢Non-essential amino acids: Synthesized in body and there is no diet
dependency for them
ā¢Semi-essential amino acids: Not synthesised in the body in adequate amounts
and requires dietary supplementation.
14. AA Classified on Basis of metabolic classification
ā¢Ketogenic amino acids: Only two aa are ketogenic, ex. Lysine and leucine. They
catabolically give intermediates convertible into acetyl-CoA or acetoacetyl-CoA
ā¢Glucogenic amino acids: Those aa give rise to intermediates of glycolysis or
Krebās cycle convertible by gluconeogenesis into glucose. Ex. Arg, His etc.
ā¢Mixed amino acids: There are aa, carbon skeleton of which catabolized to
produce the glycolytic intermediates as well as acetyl-CoA derivatives. Ex. Phe,
Try etc.
15. Amino-AcidsClassification Based on Side Chain Groups
ā¢Based on type of functional group (R group) present amino acids are classified
as: Aliphatic, aromatic, acidic, basic, acid amide, sulfur and cyclic amino acids.
ā¢Based on characteristic of functional group amino acids are classified as: polar
and non-polar amino acids.
ā¢Based on site of attachment of functional group. They are also classified as:
alpha, beta, gamma and delta amino acids.
17. Table 3.1. Harperās Illustrated Biochemistry 30 edition
Branching in isobutyl side chain on Ī³ carbon of amino
acid
Branching in isobutyl side chain on Ī² carbon of amino
acid
Nonpolar/Hydrophobic
Methyl R group
Isopropyl R group
Cont--
Ī³ Ī²
18. Cont--
Mentioned in amino acids with aromatic rings section
Thiolmethyl/Sulfhydryl R group
Methyl ethyl thiol ether R group
Hydroxymethyl R group
Secondary Alcohol structure
Polar, uncharged-R group
Polar, uncharged-R group
Polar, uncharged-R group
Nonpolar
19. Cont--
Ī²-COOH R group
Ī³-COOH R group
Polar, Uncharged-R group
Polar, Uncharged-R group
Negatively charged R group
Negatively charged R group
21. Imino group belongs to a five-member ring
Mentioned in amino acids with basic groups section
Benzene ring R group
Phenol R group
Heterocyclic structure, indole R group
Cont--
22. Function of Essential Amino acids
Non-polar amino acids:
1. Aromatic aa:
a) Phenylalanine: precursor for tyrosine, dopamine, nor-epinephrine, epinephrine and
melanin.
ā¢Genetic disorder phenylketonuria is the inability to metabolize phenylalanine because
of a lack of phenylalanine hydroxylase.
a) Tryptophan: precursor for neurotransmitter (serotonin), hormone (melatonin) and
vitamin niacin. Trp and Tyr residues anchoring membrane proteins within cell
membrane.
ā¢Fructose malabsorption causes improper absorption of Trp in intestine causes reduced
level of Trp in blood.
23. 2. Aliphatic amino acids:
a) Alanine: Alanine synthesized from pyruvate and branched chain aa. It plays
an imp. role in glucose-alanine cycle between tissues and liver.
ā¢This cycle enables pyruvate and glutamate to be removed from muscle and
safely transported to liver.
ā¢Alteration in alanine cycle increase the level of ALT (Alanine transferases) which
linked to the development of type II diabetes.
24. b) Valine: Essential for hematopoietic stem cell (HSC) self-renewal.
ā¢In sickle-cell disease, a single glutamic acid in Ī²-globin replaced with valine because
valine is hydrophobic, whereas glutamic acid is hydrophilic, this change makes the Hb
prone to abnormal aggregation.
c) Leucine: Primary metabolic end products of leucine metabolism are acetyl-CoA and
acetoacetate. It is also a imp ketogenic aa.
ā¢Adipose and muscle tissue use leucine in the formation of sterols.
ā¢MSUD caused by deficiency of branched chain Ī±-keto acid dehydrogenase complex
leading to build-up branched chain aa and their toxic product ketoacids present in blood
and urine.
25. c) Isoleucine: diverse physiological functions, such as assisting wound healing,
detoxification of nitrogenous wastes, stimulating immune function, and promoting
secretion of several hormones.
3. Sulfur-containing aa:
a) Methionine: Substrate for other amino acids such as cysteine and taurine, versatile
compounds such as S-adenosyl methionine and antioxidant glutathione.
ā¢Homocysteine can be used to regenerate methionine or to form cysteine.
ā¢Improper conversion of methionine can lead to atherosclerosis due to accumulation of
homocysteine.
26. Polar uncharged aa:
1. Threonine: Its residue ssusceptible to numerous posttranslational
modifications.
ā¢The hydroxyl side-chain undergo O-linked glycosylation.
ā¢Threonine residues undergo phosphorylation through the action of a threonine
kinase. In its phosphorylated form, it can be referred to as phosphothreonine. Its
role in cell signal transduction and neural activity.
27. Polar Charged amino-acids:
1. Positive charge/Basic aa:
a) Histidine: precursor for histamine, an amine produced in the body necessary
for inflammation.
ā¢Histidine ammonia-lyase converts histidine into ammonia and urocanic acid.
deficiency in this enzyme in rare metabolic disorder histidinemia.
28. b) Lysine: Lysine can also contribute to protein stability as its Īµ-amino group
often participates in hydrogen bonding, salt bridges and covalent interactions to
form a Schiff base.
ā¢A second major role of lysine is in epigenetic regulation by means of histone
modification.
ā¢It plays a key role in other biological processes including; structural proteins of
connective tissues, calcium homeostasis and fatty-acid metabolism.
ā¢Due to a lack of lysine catabolism, the amino acid accumulates in plasma and
patients develop hyperlysinaemia.
29. Summary
ā¢Both Ī±-amino acids and non-Ī±-amino acids occur in nature, but proteins are
synthesized using only L-Ī±-amino acids.
ā¢The R groups of amino acids determine their unique biochemical functions.
ā¢Amino acids are classified as basic, acidic, aromatic, aliphatic,
containing based on the composition and properties of their R groups.
or sulfur-
30. Reference Books
1) Harperās Illustrated Biochemistry-30th edition
2) Textbook of Biochemistry with Clinical Correlations. 4th edition. Thomas M. Devlin.
3) Biochemistry. 4th edition. Donald Voet and Judith G. Voet.
4) Biochemistry 7th edition by Jeremy M. Berg, John L. Tymoczko and Lubert Stryer
5) Lehninger Principles of Biochemistry
6) Netter's essential biochemistry 1st Ed
7) https://en.wikipedia.org/wiki/aminoacids
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