This document discusses energy transformations in biology. It begins by explaining that energy transformations are linked to chemical reactions in cells, and the laws of thermodynamics apply. ATP plays a key role by capturing free energy from exergonic reactions and transferring it to power endergonic reactions. Enzymes lower the activation energy of reactions and are highly specific biological catalysts that use several mechanisms to facilitate chemical transformations in living systems. Enzyme activity can be regulated by inhibitors binding to the active site.
This document provides an overview of metabolism and metabolic reactions. It begins by defining the key concepts of kinetic and potential energy. It then explains the laws of thermodynamics and how they apply to biological systems. Specifically, it states that energy cannot be created or destroyed, and that entropy increases with energy transfers. It introduces the idea of exergonic and endergonic reactions, and how cells harness energy from exergonic reactions through ATP. The document outlines metabolic pathways and explains how enzymes function as catalysts to lower the activation energy of reactions. It also discusses factors that regulate enzyme activity such as substrate concentration, temperature, pH, and cellular mechanisms like phosphorylation.
This document provides an overview of metabolism and oxidative phosphorylation. It defines oxidative phosphorylation as the formation of ATP using energy released by electron transfer through electron carriers in the mitochondrial inner membrane. A proton gradient couples ATP formation to electron transfer. Catabolic pathways break down molecules and release energy, while anabolic pathways use energy to build molecules. ATP powers cellular work by coupling exergonic reactions that release energy to endergonic reactions that require energy. Enzymes lower the activation energy of reactions and increase their rates.
This document discusses bioenergetics, which describes how living organisms capture, transform, store, and utilize energy. It defines endergonic and exergonic reactions, and explains that ATP is used to transport energy in cells. When ATP is hydrolyzed, energy is released to power cellular work in an exergonic reaction. This hydrolysis is coupled to endergonic reactions through common intermediates like ATP to drive biochemical pathways.
The document discusses bioenergetics, which is the study of energy transformations that occur within living cells. It covers several key topics:
- Bioenergetics obeys the laws of thermodynamics, particularly the first law of conservation of energy and the second law regarding entropy.
- Key thermodynamic concepts discussed include entropy, enthalpy, free energy, and how biological reactions are either exergonic (releasing energy) or endergonic (requiring energy).
- For a reaction to be spontaneous, the change in free energy (ΔG) must be negative. However, many essential biological reactions are non-spontaneous (endergonic).
- Cells overcome
This document discusses biomolecules and bioenergetics. It defines biomolecules as proteins and amino acids. It then discusses bioenergetics, including the concepts of free energy, endergonic and exergonic reactions. It explains how ATP is an important energy currency for cells and is regenerated through coupled reactions like substrate-level phosphorylation and oxidative phosphorylation in the mitochondria. These coupled reactions involve the exergonic hydrolysis of ATP being linked to endergonic processes like dehydration through the transfer of a phosphate group.
This document provides an overview of metabolism and metabolic reactions. It begins by defining the key concepts of kinetic and potential energy. It then explains the laws of thermodynamics and how they apply to biological systems. Specifically, it states that energy cannot be created or destroyed, and that entropy increases with energy transfers. It introduces the idea of exergonic and endergonic reactions, and how cells harness energy from exergonic reactions through ATP. The document outlines metabolic pathways and explains how enzymes function as catalysts to lower the activation energy of reactions. It also discusses factors that regulate enzyme activity such as substrate concentration, temperature, pH, and cellular mechanisms like phosphorylation.
This document provides an overview of metabolism and oxidative phosphorylation. It defines oxidative phosphorylation as the formation of ATP using energy released by electron transfer through electron carriers in the mitochondrial inner membrane. A proton gradient couples ATP formation to electron transfer. Catabolic pathways break down molecules and release energy, while anabolic pathways use energy to build molecules. ATP powers cellular work by coupling exergonic reactions that release energy to endergonic reactions that require energy. Enzymes lower the activation energy of reactions and increase their rates.
This document discusses bioenergetics, which describes how living organisms capture, transform, store, and utilize energy. It defines endergonic and exergonic reactions, and explains that ATP is used to transport energy in cells. When ATP is hydrolyzed, energy is released to power cellular work in an exergonic reaction. This hydrolysis is coupled to endergonic reactions through common intermediates like ATP to drive biochemical pathways.
The document discusses bioenergetics, which is the study of energy transformations that occur within living cells. It covers several key topics:
- Bioenergetics obeys the laws of thermodynamics, particularly the first law of conservation of energy and the second law regarding entropy.
- Key thermodynamic concepts discussed include entropy, enthalpy, free energy, and how biological reactions are either exergonic (releasing energy) or endergonic (requiring energy).
- For a reaction to be spontaneous, the change in free energy (ΔG) must be negative. However, many essential biological reactions are non-spontaneous (endergonic).
- Cells overcome
This document discusses biomolecules and bioenergetics. It defines biomolecules as proteins and amino acids. It then discusses bioenergetics, including the concepts of free energy, endergonic and exergonic reactions. It explains how ATP is an important energy currency for cells and is regenerated through coupled reactions like substrate-level phosphorylation and oxidative phosphorylation in the mitochondria. These coupled reactions involve the exergonic hydrolysis of ATP being linked to endergonic processes like dehydration through the transfer of a phosphate group.
The document summarizes key concepts about chemical reactions, energy in reactions, enzymes, and enzyme action from a biology textbook chapter on chemistry of life. It defines chemical reactions as processes that transform chemicals, with reactants entering and products forming. Reactions can release or absorb energy depending on differences in bond energies between reactants and products. Enzymes are protein catalysts that lower the activation energy of reactions, speeding up rates immensely and allowing life-sustaining reactions to occur efficiently. They achieve catalysis by creating an ideal microenvironment where substrates precisely bind at active sites.
This document provides an overview of biochemical thermodynamics and key concepts including enthalpy, entropy, free energy, and their relationships. It discusses how biochemical reactions are classified based on their standard free energy changes as either exergonic (spontaneous) or endergonic (non-spontaneous). The role of ATP as the main energy currency in cells is explained. Redox potentials of electron transport chain components are provided. Important energy-rich compounds in biological systems like ATP, phosphocreatine, and acetyl CoA are introduced along with their structures and significance.
UNIT1.2 bioenergetic in introduction of biochemistrypayalpilaji
The document discusses bioenergetics, which is the study of energy changes that occur during biochemical reactions in living organisms. It covers several key topics:
- Adenosine triphosphate (ATP) acts as the main "energy currency" in organisms and is produced through catabolic processes to be used for biological work.
- Reactions can be exergonic (releasing energy) or endergonic (requiring energy input). Exergonic reactions like cellular respiration break ATP to power biological processes.
- Activation energy is the minimum energy needed to start a chemical reaction. Enzymes and catalysts lower this barrier to speed up reactions.
- High-energy compounds like
The document provides an overview of metabolism and energy transformations in cells. It discusses how (1) cells extract and use energy to perform work through thousands of chemical reactions organized into metabolic pathways, (2) the laws of thermodynamics govern energy transformations with energy being conserved but entropy increasing, and (3) ATP powers cellular work by coupling exergonic reactions like its hydrolysis to endergonic reactions like transport or synthesis through energy transfer.
This presentation was prepared in order to take Lecture of students in a summarised way and to provide them with the short, sweet and concise notes. It is based on PCI syllabus and is meant for B. Pharm. Second Semester...
This document discusses bioenergetics, which is the study of energy transformations that occur in living organisms. It notes that all organisms need energy for physical activities, which involve chemical reactions that obey the laws of thermodynamics. Specifically, it examines human bioenergetics and how the study of cellular and metabolic processes leads to the production and use of energy in the form of ATP. Metabolism represents the chemical changes that convert nutrients into energy and complex cell products, and involves both catabolism and anabolism. Catabolism breaks down molecules to release energy or for use in anabolism, while anabolism uses energy to construct new bonds. The pathways are in equilibrium, with catabolism providing energy and
This document provides an overview of cellular metabolism and energy transformation. It discusses key topics including:
1) Metabolism transforms matter and energy in living cells through ordered chemical reactions. Metabolic pathways involve series of enzyme-catalyzed steps that either release (catabolism) or consume (anabolism) energy.
2) ATP is the main energy currency molecule in cells. It is regenerated through catabolic pathways and powers cellular work through exergonic hydrolysis reactions that drive endergonic processes.
3) Enzymes are protein catalysts that lower the activation energy of metabolic reactions, speeding up biochemical transformations without being consumed in the process. They confer specificity to reactions by precisely
The document discusses key concepts in bioenergetics including:
1) Bioenergetics concerns the energy involved in making and breaking chemical bonds in molecules, which is fundamental to biological processes like growth that depend on energy transformations.
2) The first law of thermodynamics states that energy is conserved, while the second law states that entropy increases, reducing the available free energy.
3) Free energy (G) expresses the energy available to do work and depends on enthalpy (H) and entropy (S) changes. Exergonic reactions release free energy while endergonic reactions absorb it.
The document provides an overview of metabolism and energy transformation in cells. It discusses key concepts including:
1) Metabolism transforms matter and energy through chemical reactions catalyzed by enzymes. Metabolic pathways are organized to either release or absorb energy through catabolic and anabolic reactions.
2) ATP powers cellular work by coupling exergonic reactions like ATP hydrolysis to endergonic reactions like biosynthesis. Enzymes lower the activation energy of reactions and speed up metabolic pathways.
3) The first and second laws of thermodynamics govern energy transformations in cells. Free energy changes determine whether reactions are spontaneous. While cells increase disorder, living organisms maintain local reductions in entropy.
This document provides an overview of metabolism and enzymology. It discusses how metabolism transforms matter and energy through chemical reactions, with some reactions releasing energy (catabolic pathways) and others requiring energy (anabolic pathways). ATP is used to power cellular work by transferring phosphate groups from exergonic reactions. Enzymes lower the activation energy of metabolic reactions and increase their rates. They are regulated by factors like temperature, pH, inhibitors, and feedback inhibition of pathway end products. Key organelles like mitochondria contain localized enzymes for metabolic pathways like cellular respiration.
This document discusses bioenergetics and the role of ATP in living systems. It explains that ATP stores and transports chemical energy within cells, which is released through its hydrolysis into ADP and phosphate. The hydrolysis of ATP is highly exergonic, with a large negative standard free energy change of -30.5 kJ/mol. This energy from ATP hydrolysis drives endergonic biochemical reactions and processes, such as the synthesis of glucose-6-phosphate from glucose and phosphate. The energy from ATP hydrolysis is efficiently coupled to these endergonic reactions through a cyclic process of ATP synthesis and breakdown.
- Metabolism involves chemical reactions that build up or break down molecules, organized into metabolic pathways with multiple enzyme-catalyzed steps.
- Catabolic pathways break down molecules and release energy, while anabolic pathways use energy to build molecules.
- ATP powers cellular work by coupling exergonic reactions, which release energy, to endergonic reactions like transport and synthesis that require energy. ATP is regenerated through catabolic pathways.
Organic reactions occur between organic molecules containing carbon and hydrogen. There are several types of organic reactions including addition, elimination, substitution, and rearrangement. Organic reactions are also classified by reaction type such as acid-base reactions and redox reactions. Reactions proceed through the formation of unstable intermediates like carbocations, carbanions, free radicals, and radical ions before products form. Factors like energetics, electronic effects, steric effects, stereoelectronic effects, solvent effects influence organic reactions. Reactions require activation energy to reach a transition state before products form.
1. Metabolism transforms matter and energy through chemical reactions within organisms, subject to the laws of thermodynamics. 2. Metabolic pathways are organized into catabolic pathways that break down molecules and release energy, and anabolic pathways that use energy to build molecules. 3. ATP powers cellular work by coupling exergonic reactions like its own hydrolysis to drive endergonic reactions like protein synthesis.
1) Bioenergetics examines the energy flow in living organisms using concepts like entropy, enthalpy, and free energy.
2) ATP acts as the energy currency of cells, being produced through exergonic reactions and consumed to power endergonic reactions.
3) Standard free energy changes can be added for coupled reactions and actual free energy depends on reactant and product concentrations, driving reactions towards or away from equilibrium.
Unit 4 Metabolism & matabolic disorder (3).pdfAlemu Chemeda
This document provides information about cellular metabolism and metabolic disorders. It discusses cellular metabolism, which involves chemical reactions that provide energy and synthesize new materials within cells. These reactions are divided into catabolic reactions that release energy and anabolic reactions that use energy to build molecules. The main metabolic pathways discussed are glycolysis, the citric acid (TCA) cycle, and the electron transport chain (ETC). It also covers enzymes and their role in speeding up metabolic reactions, as well as factors that affect enzymatic activity such as temperature, pH, substrate and enzyme concentration, and enzyme inhibitors.
Unit 4 Metabolism & matabolic disorder.pdfAlemu Chemeda
This document provides information about cellular metabolism and metabolic disorders. It discusses cellular metabolism, which involves chemical reactions that provide energy and synthesize new materials within cells. These reactions are divided into catabolic reactions that release energy and anabolic reactions that use energy to build larger molecules. The main metabolic pathways discussed are glycolysis, the citric acid (TCA) cycle, and the electron transport chain (ETC). Enzymes play a key role in speeding up metabolic reactions. Factors like temperature, pH, substrate and enzyme concentrations can affect enzymatic activity. The document also briefly discusses metabolic disorders.
This document provides an overview and introduction to enzymes. It discusses key properties of enzymes including their ability to act as highly effective catalysts with great reaction specificity. Enzymes are usually proteins that catalyze chemical reactions and contain active sites where substrates bind. The document outlines different classes of enzymes and explains how many require cofactors to be catalytically active. It also summarizes important thermodynamic concepts like free energy, equilibrium, and how enzymes are able to increase reaction rates by lowering the activation energy without changing the free energy change of the overall reaction.
1) Dr. Khalid Alsharafa studies plant stress physiology, including how plants sense and respond to stresses like high light, temperature extremes, heavy metals, salinity, drought, and pathogens.
2) Plants have developed strategies to respond to stress, such as lowering reactive oxygen species production, scavenging ROS through antioxidants and enzymes, and signal transduction pathways that trigger stress responses.
3) Dr. Alsharafa's research aims to analyze post-transcriptional regulation of enzyme activity under abiotic stress of different durations and intensities, monitor plant acclimation to biotic and abiotic stresses over time, and detect retrograde signaling in response to abiotic stress.
Somatic hybridization involves fusing plant cell protoplasts (naked plant cells without cell walls) from two different plant species or varieties. This is done through isolating protoplasts enzymatically, fusing them using chemicals or electricity, selecting hybrid cells, culturing the hybrid cells, and regenerating hybrid plants. Somatic hybridization allows for the transfer of useful traits like disease resistance between sexually incompatible plant species. It has been used to create novel crop hybrids and backcross fertile somatic hybrids in plants like citrus and potatoes.
More Related Content
Similar to Lecture-6 Energy, Enzymes, and Metabolism.ppt
The document summarizes key concepts about chemical reactions, energy in reactions, enzymes, and enzyme action from a biology textbook chapter on chemistry of life. It defines chemical reactions as processes that transform chemicals, with reactants entering and products forming. Reactions can release or absorb energy depending on differences in bond energies between reactants and products. Enzymes are protein catalysts that lower the activation energy of reactions, speeding up rates immensely and allowing life-sustaining reactions to occur efficiently. They achieve catalysis by creating an ideal microenvironment where substrates precisely bind at active sites.
This document provides an overview of biochemical thermodynamics and key concepts including enthalpy, entropy, free energy, and their relationships. It discusses how biochemical reactions are classified based on their standard free energy changes as either exergonic (spontaneous) or endergonic (non-spontaneous). The role of ATP as the main energy currency in cells is explained. Redox potentials of electron transport chain components are provided. Important energy-rich compounds in biological systems like ATP, phosphocreatine, and acetyl CoA are introduced along with their structures and significance.
UNIT1.2 bioenergetic in introduction of biochemistrypayalpilaji
The document discusses bioenergetics, which is the study of energy changes that occur during biochemical reactions in living organisms. It covers several key topics:
- Adenosine triphosphate (ATP) acts as the main "energy currency" in organisms and is produced through catabolic processes to be used for biological work.
- Reactions can be exergonic (releasing energy) or endergonic (requiring energy input). Exergonic reactions like cellular respiration break ATP to power biological processes.
- Activation energy is the minimum energy needed to start a chemical reaction. Enzymes and catalysts lower this barrier to speed up reactions.
- High-energy compounds like
The document provides an overview of metabolism and energy transformations in cells. It discusses how (1) cells extract and use energy to perform work through thousands of chemical reactions organized into metabolic pathways, (2) the laws of thermodynamics govern energy transformations with energy being conserved but entropy increasing, and (3) ATP powers cellular work by coupling exergonic reactions like its hydrolysis to endergonic reactions like transport or synthesis through energy transfer.
This presentation was prepared in order to take Lecture of students in a summarised way and to provide them with the short, sweet and concise notes. It is based on PCI syllabus and is meant for B. Pharm. Second Semester...
This document discusses bioenergetics, which is the study of energy transformations that occur in living organisms. It notes that all organisms need energy for physical activities, which involve chemical reactions that obey the laws of thermodynamics. Specifically, it examines human bioenergetics and how the study of cellular and metabolic processes leads to the production and use of energy in the form of ATP. Metabolism represents the chemical changes that convert nutrients into energy and complex cell products, and involves both catabolism and anabolism. Catabolism breaks down molecules to release energy or for use in anabolism, while anabolism uses energy to construct new bonds. The pathways are in equilibrium, with catabolism providing energy and
This document provides an overview of cellular metabolism and energy transformation. It discusses key topics including:
1) Metabolism transforms matter and energy in living cells through ordered chemical reactions. Metabolic pathways involve series of enzyme-catalyzed steps that either release (catabolism) or consume (anabolism) energy.
2) ATP is the main energy currency molecule in cells. It is regenerated through catabolic pathways and powers cellular work through exergonic hydrolysis reactions that drive endergonic processes.
3) Enzymes are protein catalysts that lower the activation energy of metabolic reactions, speeding up biochemical transformations without being consumed in the process. They confer specificity to reactions by precisely
The document discusses key concepts in bioenergetics including:
1) Bioenergetics concerns the energy involved in making and breaking chemical bonds in molecules, which is fundamental to biological processes like growth that depend on energy transformations.
2) The first law of thermodynamics states that energy is conserved, while the second law states that entropy increases, reducing the available free energy.
3) Free energy (G) expresses the energy available to do work and depends on enthalpy (H) and entropy (S) changes. Exergonic reactions release free energy while endergonic reactions absorb it.
The document provides an overview of metabolism and energy transformation in cells. It discusses key concepts including:
1) Metabolism transforms matter and energy through chemical reactions catalyzed by enzymes. Metabolic pathways are organized to either release or absorb energy through catabolic and anabolic reactions.
2) ATP powers cellular work by coupling exergonic reactions like ATP hydrolysis to endergonic reactions like biosynthesis. Enzymes lower the activation energy of reactions and speed up metabolic pathways.
3) The first and second laws of thermodynamics govern energy transformations in cells. Free energy changes determine whether reactions are spontaneous. While cells increase disorder, living organisms maintain local reductions in entropy.
This document provides an overview of metabolism and enzymology. It discusses how metabolism transforms matter and energy through chemical reactions, with some reactions releasing energy (catabolic pathways) and others requiring energy (anabolic pathways). ATP is used to power cellular work by transferring phosphate groups from exergonic reactions. Enzymes lower the activation energy of metabolic reactions and increase their rates. They are regulated by factors like temperature, pH, inhibitors, and feedback inhibition of pathway end products. Key organelles like mitochondria contain localized enzymes for metabolic pathways like cellular respiration.
This document discusses bioenergetics and the role of ATP in living systems. It explains that ATP stores and transports chemical energy within cells, which is released through its hydrolysis into ADP and phosphate. The hydrolysis of ATP is highly exergonic, with a large negative standard free energy change of -30.5 kJ/mol. This energy from ATP hydrolysis drives endergonic biochemical reactions and processes, such as the synthesis of glucose-6-phosphate from glucose and phosphate. The energy from ATP hydrolysis is efficiently coupled to these endergonic reactions through a cyclic process of ATP synthesis and breakdown.
- Metabolism involves chemical reactions that build up or break down molecules, organized into metabolic pathways with multiple enzyme-catalyzed steps.
- Catabolic pathways break down molecules and release energy, while anabolic pathways use energy to build molecules.
- ATP powers cellular work by coupling exergonic reactions, which release energy, to endergonic reactions like transport and synthesis that require energy. ATP is regenerated through catabolic pathways.
Organic reactions occur between organic molecules containing carbon and hydrogen. There are several types of organic reactions including addition, elimination, substitution, and rearrangement. Organic reactions are also classified by reaction type such as acid-base reactions and redox reactions. Reactions proceed through the formation of unstable intermediates like carbocations, carbanions, free radicals, and radical ions before products form. Factors like energetics, electronic effects, steric effects, stereoelectronic effects, solvent effects influence organic reactions. Reactions require activation energy to reach a transition state before products form.
1. Metabolism transforms matter and energy through chemical reactions within organisms, subject to the laws of thermodynamics. 2. Metabolic pathways are organized into catabolic pathways that break down molecules and release energy, and anabolic pathways that use energy to build molecules. 3. ATP powers cellular work by coupling exergonic reactions like its own hydrolysis to drive endergonic reactions like protein synthesis.
1) Bioenergetics examines the energy flow in living organisms using concepts like entropy, enthalpy, and free energy.
2) ATP acts as the energy currency of cells, being produced through exergonic reactions and consumed to power endergonic reactions.
3) Standard free energy changes can be added for coupled reactions and actual free energy depends on reactant and product concentrations, driving reactions towards or away from equilibrium.
Unit 4 Metabolism & matabolic disorder (3).pdfAlemu Chemeda
This document provides information about cellular metabolism and metabolic disorders. It discusses cellular metabolism, which involves chemical reactions that provide energy and synthesize new materials within cells. These reactions are divided into catabolic reactions that release energy and anabolic reactions that use energy to build molecules. The main metabolic pathways discussed are glycolysis, the citric acid (TCA) cycle, and the electron transport chain (ETC). It also covers enzymes and their role in speeding up metabolic reactions, as well as factors that affect enzymatic activity such as temperature, pH, substrate and enzyme concentration, and enzyme inhibitors.
Unit 4 Metabolism & matabolic disorder.pdfAlemu Chemeda
This document provides information about cellular metabolism and metabolic disorders. It discusses cellular metabolism, which involves chemical reactions that provide energy and synthesize new materials within cells. These reactions are divided into catabolic reactions that release energy and anabolic reactions that use energy to build larger molecules. The main metabolic pathways discussed are glycolysis, the citric acid (TCA) cycle, and the electron transport chain (ETC). Enzymes play a key role in speeding up metabolic reactions. Factors like temperature, pH, substrate and enzyme concentrations can affect enzymatic activity. The document also briefly discusses metabolic disorders.
This document provides an overview and introduction to enzymes. It discusses key properties of enzymes including their ability to act as highly effective catalysts with great reaction specificity. Enzymes are usually proteins that catalyze chemical reactions and contain active sites where substrates bind. The document outlines different classes of enzymes and explains how many require cofactors to be catalytically active. It also summarizes important thermodynamic concepts like free energy, equilibrium, and how enzymes are able to increase reaction rates by lowering the activation energy without changing the free energy change of the overall reaction.
Similar to Lecture-6 Energy, Enzymes, and Metabolism.ppt (20)
1) Dr. Khalid Alsharafa studies plant stress physiology, including how plants sense and respond to stresses like high light, temperature extremes, heavy metals, salinity, drought, and pathogens.
2) Plants have developed strategies to respond to stress, such as lowering reactive oxygen species production, scavenging ROS through antioxidants and enzymes, and signal transduction pathways that trigger stress responses.
3) Dr. Alsharafa's research aims to analyze post-transcriptional regulation of enzyme activity under abiotic stress of different durations and intensities, monitor plant acclimation to biotic and abiotic stresses over time, and detect retrograde signaling in response to abiotic stress.
Somatic hybridization involves fusing plant cell protoplasts (naked plant cells without cell walls) from two different plant species or varieties. This is done through isolating protoplasts enzymatically, fusing them using chemicals or electricity, selecting hybrid cells, culturing the hybrid cells, and regenerating hybrid plants. Somatic hybridization allows for the transfer of useful traits like disease resistance between sexually incompatible plant species. It has been used to create novel crop hybrids and backcross fertile somatic hybrids in plants like citrus and potatoes.
This document discusses different methods for predicting the secondary structure of proteins, including statistical methods like Chou-Fasman and GOR that use amino acid frequencies, and neural network methods like PHD that use multiple sequence alignments and training sets of known structures. It also briefly outlines experimental methods for determining protein structure like X-ray crystallography, NMR spectroscopy, and cryo-electron microscopy.
- Evolution is the process of change over generations in inherited traits of organisms due to mutations, genetic recombination, and natural selection.
- Molecular phylogeny uses DNA and protein sequences to reconstruct evolutionary relationships and depict them in phylogenetic trees.
- Phylogenetic trees show how taxa are related through time with internal nodes representing common ancestors and branches representing elapsed time or genetic changes between nodes. Well-constructed phylogenetic trees are important for understanding the evolution and classification of living things.
Mendeley is a free reference manager and academic social network that can help researchers organize, share, and discover research papers. It allows users to create a personal library by adding papers from their computer or online resources, collaborate with other researchers, and generate citations and bibliographies in Microsoft Word, OpenOffice, and LaTeX. The presentation introduced Mendeley's core features like adding documents, managing metadata, annotating papers, citing as you write, and synchronizing a library online.
The document discusses different modern methods of plant breeding including mutation breeding, polyploidy breeding, and haploidy breeding. It provides details on mutation breeding including how mutagens like radiation and chemicals can induce mutations and the process of mutation breeding from selection of material to development of new varieties. It also describes polyploidy breeding which involves variations in chromosome number like polyploids having more than two sets of genomes. Finally, it mentions how haploids which have only one set of chromosomes can be used in plant breeding through techniques like haploid production and chromosome doubling.
1. Glycolysis is a pathway that takes place in the cytosol of cells and involves the breakdown of glucose to pyruvate. It involves 10 enzyme-catalyzed steps and results in the production of ATP.
2. The first three steps involve phosphorylation of glucose to glucose-6-phosphate by hexokinase, isomerization to fructose-6-phosphate by phosphoglucose isomerase, and phosphorylation to fructose-1,6-bisphosphate by phosphofructokinase.
3. Subsequent steps break down the six-carbon glucose into two three-carbon molecules, convert them to pyruvate, and generate ATP through substrate-level phosphorylation
Cell Therapy Expansion and Challenges in Autoimmune DiseaseHealth Advances
There is increasing confidence that cell therapies will soon play a role in the treatment of autoimmune disorders, but the extent of this impact remains to be seen. Early readouts on autologous CAR-Ts in lupus are encouraging, but manufacturing and cost limitations are likely to restrict access to highly refractory patients. Allogeneic CAR-Ts have the potential to broaden access to earlier lines of treatment due to their inherent cost benefits, however they will need to demonstrate comparable or improved efficacy to established modalities.
In addition to infrastructure and capacity constraints, CAR-Ts face a very different risk-benefit dynamic in autoimmune compared to oncology, highlighting the need for tolerable therapies with low adverse event risk. CAR-NK and Treg-based therapies are also being developed in certain autoimmune disorders and may demonstrate favorable safety profiles. Several novel non-cell therapies such as bispecific antibodies, nanobodies, and RNAi drugs, may also offer future alternative competitive solutions with variable value propositions.
Widespread adoption of cell therapies will not only require strong efficacy and safety data, but also adapted pricing and access strategies. At oncology-based price points, CAR-Ts are unlikely to achieve broad market access in autoimmune disorders, with eligible patient populations that are potentially orders of magnitude greater than the number of currently addressable cancer patients. Developers have made strides towards reducing cell therapy COGS while improving manufacturing efficiency, but payors will inevitably restrict access until more sustainable pricing is achieved.
Despite these headwinds, industry leaders and investors remain confident that cell therapies are poised to address significant unmet need in patients suffering from autoimmune disorders. However, the extent of this impact on the treatment landscape remains to be seen, as the industry rapidly approaches an inflection point.
TEST BANK For Basic and Clinical Pharmacology, 14th Edition by Bertram G. Kat...rightmanforbloodline
TEST BANK For Basic and Clinical Pharmacology, 14th Edition by Bertram G. Katzung, Verified Chapters 1 - 66, Complete Newest Version.
TEST BANK For Basic and Clinical Pharmacology, 14th Edition by Bertram G. Katzung, Verified Chapters 1 - 66, Complete Newest Version.
TEST BANK For Basic and Clinical Pharmacology, 14th Edition by Bertram G. Katzung, Verified Chapters 1 - 66, Complete Newest Version.
TEST BANK For Basic and Clinical Pharmacology, 14th Edition by Bertram G. Katzung, Verified Chapters 1 - 66, Complete Newest Version.
share - Lions, tigers, AI and health misinformation, oh my!.pptxTina Purnat
• Pitfalls and pivots needed to use AI effectively in public health
• Evidence-based strategies to address health misinformation effectively
• Building trust with communities online and offline
• Equipping health professionals to address questions, concerns and health misinformation
• Assessing risk and mitigating harm from adverse health narratives in communities, health workforce and health system
These lecture slides, by Dr Sidra Arshad, offer a quick overview of the physiological basis of a normal electrocardiogram.
Learning objectives:
1. Define an electrocardiogram (ECG) and electrocardiography
2. Describe how dipoles generated by the heart produce the waveforms of the ECG
3. Describe the components of a normal electrocardiogram of a typical bipolar lead (limb II)
4. Differentiate between intervals and segments
5. Enlist some common indications for obtaining an ECG
6. Describe the flow of current around the heart during the cardiac cycle
7. Discuss the placement and polarity of the leads of electrocardiograph
8. Describe the normal electrocardiograms recorded from the limb leads and explain the physiological basis of the different records that are obtained
9. Define mean electrical vector (axis) of the heart and give the normal range
10. Define the mean QRS vector
11. Describe the axes of leads (hexagonal reference system)
12. Comprehend the vectorial analysis of the normal ECG
13. Determine the mean electrical axis of the ventricular QRS and appreciate the mean axis deviation
14. Explain the concepts of current of injury, J point, and their significance
Study Resources:
1. Chapter 11, Guyton and Hall Textbook of Medical Physiology, 14th edition
2. Chapter 9, Human Physiology - From Cells to Systems, Lauralee Sherwood, 9th edition
3. Chapter 29, Ganong’s Review of Medical Physiology, 26th edition
4. Electrocardiogram, StatPearls - https://www.ncbi.nlm.nih.gov/books/NBK549803/
5. ECG in Medical Practice by ABM Abdullah, 4th edition
6. Chapter 3, Cardiology Explained, https://www.ncbi.nlm.nih.gov/books/NBK2214/
7. ECG Basics, http://www.nataliescasebook.com/tag/e-c-g-basics
TEST BANK For An Introduction to Brain and Behavior, 7th Edition by Bryan Kol...rightmanforbloodline
TEST BANK For An Introduction to Brain and Behavior, 7th Edition by Bryan Kolb, Ian Q. Whishaw, Verified Chapters 1 - 16, Complete Newest Versio
TEST BANK For An Introduction to Brain and Behavior, 7th Edition by Bryan Kolb, Ian Q. Whishaw, Verified Chapters 1 - 16, Complete Newest Version
TEST BANK For An Introduction to Brain and Behavior, 7th Edition by Bryan Kolb, Ian Q. Whishaw, Verified Chapters 1 - 16, Complete Newest Version
Promoting Wellbeing - Applied Social Psychology - Psychology SuperNotesPsychoTech Services
A proprietary approach developed by bringing together the best of learning theories from Psychology, design principles from the world of visualization, and pedagogical methods from over a decade of training experience, that enables you to: Learn better, faster!
Histololgy of Female Reproductive System.pptxAyeshaZaid1
Dive into an in-depth exploration of the histological structure of female reproductive system with this comprehensive lecture. Presented by Dr. Ayesha Irfan, Assistant Professor of Anatomy, this presentation covers the Gross anatomy and functional histology of the female reproductive organs. Ideal for students, educators, and anyone interested in medical science, this lecture provides clear explanations, detailed diagrams, and valuable insights into female reproductive system. Enhance your knowledge and understanding of this essential aspect of human biology.
2. Energy, Enzymes, and Metabolism
• What Physical Principles Underlie
Biological Energy Transformations?
• What Is the Role of ATP in Biochemical
Energetics?
• What Are Enzymes?
• How Do Enzymes Work?
• How Are Enzyme Activities Regulated?
3. What Physical Principles Underlie Biological Energy
Transformations?
The transformation of energy is a
hallmark of life.
Energy is the capacity to do work, or the
capacity for change.
Energy transformations are linked to
chemical transformations in cells.
4. 8.1 What Physical Principles Underlie Biological Energy
Transformations?
All forms of energy can be placed in two
categories:
• Potential energy is stored energy—as
chemical bonds, concentration gradient,
charge imbalance, etc.
• Kinetic energy is the energy of
movement
5. What Physical Principles Underlie Biological Energy
Transformations?
The laws of thermodynamics (thermo,
“energy”; dynamics, “change”) apply to all
matter and all energy transformations in
the universe.
They help us to understand how cells
harvest and transform energy to sustain
life.
6. What Physical Principles Underlie Biological Energy
Transformations?
First law of thermodynamics: Energy is
neither created nor destroyed.
When energy is converted from one form
to another, the total energy before and
after the conversion is the same.
7. What Physical Principles Underlie Biological Energy
Transformations?
Second law of thermodynamics: When
energy is converted from one form to
another, some of that energy becomes
unavailable to do work.
No energy transformation is 100 percent
efficient.
9. What Physical Principles Underlie Biological Energy
Transformations?
Entropy is a measure of the disorder in a
system.
It takes energy to impose order on a
system. Unless energy is applied to a
system, it will be randomly arranged or
disordered.
10. What Physical Principles Underlie Biological Energy
Transformations?
In any system:
Total energy = usable energy + unusable energy
enthalpy (H) = free energy (G) + entropy (S)
or H = G + TS (T = absolute temperature)
G = H – TS
11. What Physical Principles Underlie Biological Energy
Transformations?
Change in energy can be measured in
calories or joules.
Change in free energy (ΔG) in a reaction
is the difference in free energy of the
products and the reactants.
12. What Physical Principles Underlie Biological Energy
Transformations?
ΔG = ΔH – TΔS
• If ΔG is negative, free energy is
released
• If ΔG is positive, free energy is
consumed
If free energy is not available, the
reaction does not occur.
13. What Physical Principles Underlie Biological Energy
Transformations?
Magnitude of ΔG depends on:
• ΔH—total energy added (ΔH > 0) or
released (ΔH < 0)
• ΔS—change in entropy. Large changes
in entropy make ΔG more negative
14. What Physical Principles Underlie Biological Energy
Transformations?
If a chemical reaction increases entropy,
the products will be more disordered.
Example: In hydrolysis of a protein into its
component amino acids, ΔS is positive.
15. What Physical Principles Underlie Biological Energy
Transformations?
Second law of thermodynamics:
Disorder tends to increase because of
energy transformations.
Living organisms must have a constant
supply of energy to maintain order.
16. What Physical Principles Underlie Biological Energy
Transformations?
Metabolism: Sum total of all chemical
reactions in an organism.
Anabolic reactions: Complex molecules
are made from simple molecules; energy
input is required.
Catabolic reactions: Complex molecules
are broken down to simpler ones and
energy is released.
17. What Physical Principles Underlie Biological Energy
Transformations?
Exergonic reactions release free energy
(–ΔG): Catabolism; complexity
decreases (generates disorder).
Endergonic reactions consume free
energy (+ΔG): anabolism; complexity
(order) increases.
20. 8.1 What Physical Principles Underlie Biological Energy
Transformations?
In principle, chemical reactions can run in
both directions.
At chemical equilibrium, ΔG = 0
Forward and reverse reactions are
balanced.
The concentrations of A and B determine
which direction will be favored.
B
A
21. What Physical Principles Underlie Biological Energy
Transformations?
Every reaction has a specific equilibrium
point.
ΔG is related to the point of equilibrium:
The further towards completion the point
of equilibrium is, the more free energy is
released.
ΔG values near zero are characteristic of
readily reversible reactions.
23. 8.2 What Is the Role of ATP in Biochemical Energetics?
ATP (adenosine triphosphate) captures
and transfers free energy.
ATP releases a large amount of energy
when hydrolyzed.
ATP can phosphorylate, or donate
phosphate groups to other molecules.
24. 8.2 What Is the Role of ATP in Biochemical Energetics?
ATP is a nucleotide.
Hydrolysis of ATP yields free energy.
ΔG = –7.3 to –14 kcal/mol
(exergonic)
energy
free
P
ADP
O
H
ATP i
2
26. 8.2 What Is the Role of ATP in Biochemical Energetics?
Bioluminescence is an endergonic
reaction driven by ATP hydrolysis:
light
PP
AMP
in
oxylucifer
ATP
O
luciferin
i
luciferase
2
28. What Is the Role of ATP in Biochemical Energetics?
The formation of ATP is endergonic:
Formation and hydrolysis of ATP couples
exergonic and endergonic reactions.
O
H
ATP
energy
free
P
ADP i 2
29. Energy Coupling
• Living organisms have the ability to couple
exergonic and endergonic reactions:
• Energy released by exergonic reactions is
captured and used to make ATP from ADP and Pi
• ATP can be broken back down to ADP and Pi,
releasing energy to power the cell’s endergonic
reactions.
30. Figure Coupling of Reactions
Exergonic and endergonic reactions are coupled.
32. What Are Enzymes?
Catalysts speed up the rate of a reaction.
The catalyst is not altered by the
reactions.
Most biological catalysts are enzymes
(proteins) that act as a framework in
which reactions can take place.
33. What Are Enzymes?
Some reactions are slow because of an
energy barrier—the amount of energy
required to start the reaction, called
activation energy (Ea).
36. What Are Enzymes?
Activation energy changes the reactants
into unstable forms with higher free
energy—transition state intermediates.
Activation energy can come from heating
the system—the reactants have more
kinetic energy.
Enzymes and ribozymes lower the energy
barrier by bringing the reactants together.
37. What Are Enzymes?
Biological catalysts (enzymes and
ribozymes) are highly specific.
Reactants are called substrates.
Substrate molecules bind to the active
site of the enzyme.
The three-dimensional shape of the
enzyme determines the specificity.
39. What Are Enzymes?
The enzyme-substrate complex (ES) is
held together by hydrogen bonds,
electrical attraction, or covalent bonds.
E + S → ES → E + P
The enzyme may change when bound to
the substrate, but returns to its original
form.
40. What Are Enzymes?
Enzymes lower the energy barrier for
reactions.
The final equilibrium doesn’t change, and
ΔG doesn’t change.
42. How Do Enzymes Work?
In catalyzing a reaction, an enzyme may
use one or more mechanisms.
43. Figure Life at the Active Site (A)
Enzymes orient substrate molecules,
bringing together the atoms that will bond.
44. Figure Life at the Active Site (B)
Enzymes can stretch the bonds in substrate
molecules, making them unstable.
45. Figure Life at the Active Site (C)
Enzymes can temporarily add chemical
groups to substrates.
46. How Do Enzymes Work?
Acid-base catalysis: Enzyme side chains
transfer H+ to or from the substrate,
causing a covalent bond to break.
Covalent catalysis: A functional group in
a side chain bonds covalently with the
substrate.
Metal ion catalysis: Metals on side chains
loose or gain electrons.
47. How Do Enzymes Work?
Shape of enzyme active site allows a
specific substrate to fit (lock and key).
Binding of substrate to the active site
depends on hydrogen bonds, attraction
and repulsion of electrically charged
groups, and hydrophobic interactions.
Many enzymes change shape when they
bind to the substrate—induced fit.
48. How Do Enzymes Work?
Some enzymes require “partners”:
• Prosthetic groups: Non-amino acid
groups bound to enzymes
• Cofactors: Inorganic ions
• Coenzymes: Small carbon-containing
molecules; not bound permanently to
enzymes
49.
50. How Do Enzymes Work?
The rate of a catalyzed reaction depends
on substrate concentration.
Concentration of an enzyme is usually
much lower than concentration of a
substrate.
At saturation, all enzyme is bound to
substrate—maximum rate.
52. How Do Enzymes Work?
Maximum rate is used to calculate
enzyme efficiency: Molecules of
substrate converted to product per unit
time (turnover).
Ranges from 1 to 40 million molecules
per second!
53. How Are Enzyme Activities Regulated?
Inhibitors regulate enzymes: Molecules
that bind to the enzyme and slow
reaction rates.
Naturally occurring inhibitors regulate
metabolism.
54. How Are Enzyme Activities Regulated?
Irreversible inhibition: Inhibitor
covalently bonds to side chains in the
active site—permanently inactivates the
enzyme.
Example: DIPF or nerve gas
Diisopropyl fluorophosphate
56. How Are Enzyme Activities Regulated?
Reversible inhibition: Inhibitor bonds
noncovalently to the active site and
prevents substrate from binding.
Competitive inhibitors compete with the
natural substrate for binding sites.
When concentration of competitive
inhibitor is reduced, it detaches from the
active site.
58. 8.5 How Are Enzyme Activities Regulated?
Noncompetitive inhibitors: Bind to the
enzyme at a different site (not the active
site).
The enzyme changes shape and alters
the active site.
60. How Are Enzyme Activities Regulated?
Allostery (allo, “different”; stereos,
“shape”)
Some enzymes exist in more than one
shape:
• Active form—can bind substrate
• Inactive form—cannot bind substrate but
can bind an inhibitor
61. How Are Enzyme Activities Regulated?
Most allosteric enzymes are proteins with
quaternary structure.
Active site is on the catalytic subunit.
Inhibitors and activators bind to the
regulatory subunits.
63. How Are Enzyme Activities Regulated?
Within a certain range, reaction rates of
allosteric enzymes are sensitive to small
changes in substrate concentration.
65. How Are Enzyme Activities Regulated?
Allosteric enzymes are very sensitive to
low concentrations of inhibitors, and are
important in regulating metabolic
pathways.
66. How Are Enzyme Activities Regulated?
Metabolic pathways:
The first reaction is the commitment
step—other reactions then happen in
sequence.
Feedback inhibition (end-product
inhibition): The final product acts as a
noncompetitive inhibitor of the first
enzyme, which shuts down the pathway.
68. 8.5 How Are Enzyme Activities Regulated?
Every enzyme is most active at a
particular pH.
pH influences the ionization of functional
groups.
Example: at low pH (high H+) —COO–
may react with H+ to form —COOH
which is no longer charged; this affects
folding and thus enzyme function.
70. 8.5 How Are Enzyme Activities Regulated?
Every enzyme has an optimal
temperature.
At high temperatures, noncovalent bonds
begin to break.
Enzyme can lose its tertiary structure and
become denatured.
72. 8.5 How Are Enzyme Activities Regulated?
Isozymes: Enzymes that catalyze the
same reaction but have different
properties, such as optimal temperature.
Organisms can use isozymes to adjust to
temperature changes.
Enzymes in humans have higher optimal
temperature than enzymes in most
bacteria—a fever can denature the
bacterial enzymes.