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... perspective of the chemical principles and chemical reactions. We will cover: 1. Biochemical structures. We will study detailed aspects of the three-dimensional structure of proteins, and how this translates into differences in the function of these proteins. 2. Energy metabolism. Biological systems ...
... perspective of the chemical principles and chemical reactions. We will cover: 1. Biochemical structures. We will study detailed aspects of the three-dimensional structure of proteins, and how this translates into differences in the function of these proteins. 2. Energy metabolism. Biological systems ...
2009 Dental Biochemistry (Questions)
... consist of phospholipids and proteins. surround cells and intracellular organelles control the entry and exit of inorganic ions, and nutrients. have same phospholipid composition on the inner and outer bilayers. maintain concentration gradients across and inside the cells ...
... consist of phospholipids and proteins. surround cells and intracellular organelles control the entry and exit of inorganic ions, and nutrients. have same phospholipid composition on the inner and outer bilayers. maintain concentration gradients across and inside the cells ...
Slide 1
... macromolecules. The most familiar type of nucleic acid is DNA or deoxyribonucleic acid. DNA is the molecule that carries all the instructions to make an organism. DNA is inherited meaning it is passed from parent to offspring. DNA is made of building blocks called nucleotides. DNA is found in the nu ...
... macromolecules. The most familiar type of nucleic acid is DNA or deoxyribonucleic acid. DNA is the molecule that carries all the instructions to make an organism. DNA is inherited meaning it is passed from parent to offspring. DNA is made of building blocks called nucleotides. DNA is found in the nu ...
Ch.3 Review Using Vocabulary a) A monomer is a simpler, smaller
... 15. An amino acid contains a central carbon atom covalently bonded to four other atoms or functional groups. A single hydrogen atom bonds at one site, a carboxyl group at a second site, an amino group at a third site, and a side chain called the R Group bonds at the fourth site. 16. Two amino acids ...
... 15. An amino acid contains a central carbon atom covalently bonded to four other atoms or functional groups. A single hydrogen atom bonds at one site, a carboxyl group at a second site, an amino group at a third site, and a side chain called the R Group bonds at the fourth site. 16. Two amino acids ...
Keystone Review Packet #2 Answers
... another molecule forming a hydrogen bond. In other words water likes to stick to itself. Water sticking to water is called cohesion. Water sticking to something else is called adhesion. ...
... another molecule forming a hydrogen bond. In other words water likes to stick to itself. Water sticking to water is called cohesion. Water sticking to something else is called adhesion. ...
Spectrophotometry, Colour and Turbidity
... Bacterial Diversity Objective To be able to describe the main features of bacterial cells and to understand the different nutritional and metabolic types. References Gray N.F. Biology of Wastewater Treatment Madigan M.T., Martinko J.M., Parker J. Brock - Biology of Microorganisms Stanier ...
... Bacterial Diversity Objective To be able to describe the main features of bacterial cells and to understand the different nutritional and metabolic types. References Gray N.F. Biology of Wastewater Treatment Madigan M.T., Martinko J.M., Parker J. Brock - Biology of Microorganisms Stanier ...
Exam II answer key
... of energy? They are more reduced and do not hydrate. This means they yield more energy per unit weight. 8. (6pts) Outline the degradation pathway for ornithine. ...
... of energy? They are more reduced and do not hydrate. This means they yield more energy per unit weight. 8. (6pts) Outline the degradation pathway for ornithine. ...
Exam II
... of energy? They are more reduced and do not hydrate. This means they yield more energy per unit weight. 8. (6pts) Outline the degradation pathway for ornithine. ...
... of energy? They are more reduced and do not hydrate. This means they yield more energy per unit weight. 8. (6pts) Outline the degradation pathway for ornithine. ...
Amino acid sequence of phospholipase A from porcine pancreas
... bonds of the molecule, as well as I asparagine and 2 tyrosine bonds. Accordingly, a total of 17 peptides were obtained containing all the residues of the original protein. After separation of these tryptic peptides on Sephadex G-25 (fine grade) and paper, their sequences were fully or partially dete ...
... bonds of the molecule, as well as I asparagine and 2 tyrosine bonds. Accordingly, a total of 17 peptides were obtained containing all the residues of the original protein. After separation of these tryptic peptides on Sephadex G-25 (fine grade) and paper, their sequences were fully or partially dete ...
ExamReview2012
... 26. Importance, structure and function in metabolic reactions of ATP 27. Uses of ATP (chemical, mechanical and transport) 28. Enzyme structure, function, specificity 29. Induced fit model of enzyme function 30. Catalytic cycles (enzyme-substrate complex) 31. Factors affecting enzyme function (temper ...
... 26. Importance, structure and function in metabolic reactions of ATP 27. Uses of ATP (chemical, mechanical and transport) 28. Enzyme structure, function, specificity 29. Induced fit model of enzyme function 30. Catalytic cycles (enzyme-substrate complex) 31. Factors affecting enzyme function (temper ...
Organic Molecules Power Point
... 1. Each unique: Used for Only 1 type Rx 2. Are reusable 3. Aren’t consumed in Rx 4. Can run Rx in reverse ...
... 1. Each unique: Used for Only 1 type Rx 2. Are reusable 3. Aren’t consumed in Rx 4. Can run Rx in reverse ...
Energy
... Every reaction within a metabolic pathway requires an enzyme ,it is organic catalysts ,usually globular protein molecules that speed chemical reactions without being permanently changed .In addition some RNA molecule particularly in the nucleus ,can be enzymes and these are called riboenzymes .Every ...
... Every reaction within a metabolic pathway requires an enzyme ,it is organic catalysts ,usually globular protein molecules that speed chemical reactions without being permanently changed .In addition some RNA molecule particularly in the nucleus ,can be enzymes and these are called riboenzymes .Every ...
Biochemistry Objectives Concepts of Matter and Energy (pp. 59
... Compare and contrast carbohydrates, lipids, proteins, and nucleic acids in terms of their building blocks, structures, and functions in the body. Differentiate between fibrous and globular proteins. Compare and contrast the structure and functions of DNA and RNA. Define enzyme and explain the role o ...
... Compare and contrast carbohydrates, lipids, proteins, and nucleic acids in terms of their building blocks, structures, and functions in the body. Differentiate between fibrous and globular proteins. Compare and contrast the structure and functions of DNA and RNA. Define enzyme and explain the role o ...
Chapter 16 - The Citric Acid Cycle
... Roles of PDH complex components •NAD+ and HS-CoA are cosubstrates •TPP, lipoate and FAD are prosthetic groups •ATP is a regulator of the PDH complex •Lipoamide (on E2) acts as a “swinging arm” to transfer the two carbon unit from the active site of E1 to the active site of E3 (substrate channeling) ...
... Roles of PDH complex components •NAD+ and HS-CoA are cosubstrates •TPP, lipoate and FAD are prosthetic groups •ATP is a regulator of the PDH complex •Lipoamide (on E2) acts as a “swinging arm” to transfer the two carbon unit from the active site of E1 to the active site of E3 (substrate channeling) ...
BIOCHEMISTRY (CHEM 360)
... (as in protease enzymes) to form an acyl intermediate? The cysteine side chain forms a thio-ester, instead of a normal ester with serine. Thio-esters are more reactive and thus more susceptible to nucleophilic attack especially since the hydrogen phosphate is a weak nucleophile. ...
... (as in protease enzymes) to form an acyl intermediate? The cysteine side chain forms a thio-ester, instead of a normal ester with serine. Thio-esters are more reactive and thus more susceptible to nucleophilic attack especially since the hydrogen phosphate is a weak nucleophile. ...
Name____________________________ Student number
... C) are very specific and can prevent the conversion of products back to substrates. D) increase the equilibrium constants for the reactions they catalyze. •E) lower the activation energy for the reactions they catalyze. 2. Which of the following statements is true of enzyme catalysts? A) To be effec ...
... C) are very specific and can prevent the conversion of products back to substrates. D) increase the equilibrium constants for the reactions they catalyze. •E) lower the activation energy for the reactions they catalyze. 2. Which of the following statements is true of enzyme catalysts? A) To be effec ...
Biochem01 - Amit Kessel Ph.D
... b) Having more than one regulated step in the pathway allows for feedback inhibition. c) Control of a single step in a reaction pathway is difficult because the concentrations of enzymes in cells are very low. It is easier to control more than one enzyme than just one. d) All the ATP in a cell would ...
... b) Having more than one regulated step in the pathway allows for feedback inhibition. c) Control of a single step in a reaction pathway is difficult because the concentrations of enzymes in cells are very low. It is easier to control more than one enzyme than just one. d) All the ATP in a cell would ...
University of - Biochemistry at the University of Maryland, College Park
... exp(−ΔG′º/RT) = {[3-PG][NADH][ATP] / [GAP][NAD+][ADP][Pi]} 157 = {(10−3 M) (10−3) (3 × 10−3) / (10−3) (10−3) (10−3) [Pi]} [Pi] = (3 × 10−3) / [(10−3) (157) = 0.0191 M (not nearly as much) 5. (20 points) Glycolysis (a; 12 points) Listed below are three enzymes from the glycolysis pathway. For any two ...
... exp(−ΔG′º/RT) = {[3-PG][NADH][ATP] / [GAP][NAD+][ADP][Pi]} 157 = {(10−3 M) (10−3) (3 × 10−3) / (10−3) (10−3) (10−3) [Pi]} [Pi] = (3 × 10−3) / [(10−3) (157) = 0.0191 M (not nearly as much) 5. (20 points) Glycolysis (a; 12 points) Listed below are three enzymes from the glycolysis pathway. For any two ...
Practice Exam II answers
... b). The distal histidine binds to oxygen and allows for the iron to be moved into the plane of the heme in a protein conformational change. c). The proximal histidine binds to oxygen and holds it in position for optimal iron binding due to a protein conformational change. d). Oxygen binds to the iro ...
... b). The distal histidine binds to oxygen and allows for the iron to be moved into the plane of the heme in a protein conformational change. c). The proximal histidine binds to oxygen and holds it in position for optimal iron binding due to a protein conformational change. d). Oxygen binds to the iro ...
Enzyme
Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions. The molecules at the beginning of the process are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life. The set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology.Enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Enzymes' specificity comes from their unique three-dimensional structures.Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal temperature and pH.Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some household products use enzymes to speed up chemical reactions: enzymes in biological washing powders break down protein, starch or fat stains on clothes, and enzymes in meat tenderizer break down proteins into smaller molecules, making the meat easier to chew.