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Questions and Answers
What is the characteristic pH at which the net electric charge of an amino acid is zero called?
What is the characteristic pH at which the net electric charge of an amino acid is zero called?
Which property describes substances that can act as both acids and bases?
Which property describes substances that can act as both acids and bases?
For glycine, how is the isoelectric point (pI) determined?
For glycine, how is the isoelectric point (pI) determined?
What role do amino acids play in relation to protons?
What role do amino acids play in relation to protons?
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What best describes the concept of enantiomers in biochemistry?
What best describes the concept of enantiomers in biochemistry?
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What is the equation that represents the formation of a holoenzyme from an apoenzyme and a cofactor?
What is the equation that represents the formation of a holoenzyme from an apoenzyme and a cofactor?
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What types of vitamins primarily function as coenzymes in biochemical reactions?
What types of vitamins primarily function as coenzymes in biochemical reactions?
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Why are coenzymes important for metabolic reactions?
Why are coenzymes important for metabolic reactions?
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What type of enzyme inhibitor binds tightly or covalently to an enzyme?
What type of enzyme inhibitor binds tightly or covalently to an enzyme?
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How do enzymes primarily affect chemical reactions?
How do enzymes primarily affect chemical reactions?
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What is the primary function of tetrahydrofolic acid (THF) in the body?
What is the primary function of tetrahydrofolic acid (THF) in the body?
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How is vitamin D synthesized and what is its primary role?
How is vitamin D synthesized and what is its primary role?
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Describe the role of vitamin K in the body.
Describe the role of vitamin K in the body.
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What is the significance of lipoic acid in metabolism?
What is the significance of lipoic acid in metabolism?
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What are the antioxidants and their main role in the body?
What are the antioxidants and their main role in the body?
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What coenzyme is formed from Vitamin B1 and what role does it play in biochemical reactions?
What coenzyme is formed from Vitamin B1 and what role does it play in biochemical reactions?
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What are the primary functions of Vitamin B2 as it relates to coenzymes?
What are the primary functions of Vitamin B2 as it relates to coenzymes?
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How does Vitamin B6 act as a coenzyme, and what type of bonds can it help cleave?
How does Vitamin B6 act as a coenzyme, and what type of bonds can it help cleave?
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What is the role of Vitamin B12 in biochemical reactions?
What is the role of Vitamin B12 in biochemical reactions?
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In what way does Nicotinamide function in redox reactions?
In what way does Nicotinamide function in redox reactions?
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What is the significance of pantothenic acid in metabolism?
What is the significance of pantothenic acid in metabolism?
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Describe the function of biotin in biochemical reactions.
Describe the function of biotin in biochemical reactions.
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What is the role of Vitamin C in collagen synthesis and overall health?
What is the role of Vitamin C in collagen synthesis and overall health?
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Study Notes
Amino Acids Overview
- Amino acids contain a central carbon atom (chiral center) bonded to an amino group (NH2), a carboxyl group (COOH), a hydrogen atom, and a variable R group (side chain).
- Amino acids can exist as enantiomers, which are mirror images of each other due to the presence of a chiral center.
Classification of Amino Acids
- Amino acids are classified based on their R groups, which determine their chemical properties, polarity, and roles in protein structure.
Amphoteric Nature
- Amino acids can act as acids (proton donors) and bases (proton acceptors), showcasing their amphoteric nature.
- Substances that exhibit this dual characteristic are referred to as ampholytes.
Titration Curves and Isoelectric Point
- The titration curves of amino acids illustrate how their electric charge changes with pH.
- The isoelectric point (pI) is the pH at which the net charge of an amino acid is zero, typically indicated by the average of the two pKa values.
- For glycine, which lacks an ionizable side chain group, the isoelectric point can be calculated directly from its pKa values.
Peptides
- Peptides are short chains of amino acids linked by peptide bonds.
- They play critical roles in biological functions and can vary significantly in length and composition.
Enzymes
- Enzymes are primarily proteins that catalyze biochemical reactions.
- They bind weakly to substrates, facilitating various biochemical processes.
Function of Enzymes
- Enzymes increase reaction rates without affecting the equilibrium position of reactions.
Catalysis Mechanisms
- Acid-Base Catalysis: Protons transfer alters substrate chemistry.
- Covalent Catalysis: Enzyme forms covalent bonds with the substrate, aiding reaction progress.
- Metal Ion Catalysis: Metal ions assist in stabilizing charged intermediates or facilitating electron transfer.
Enzyme Inhibition
- Enzyme inhibitors can block activity, affecting metabolic pathways.
Enzyme Composition
- Many enzymes need cofactors for activity, indicated by the equation: Apoenzyme + Cofactor = Holoenzyme.
- Cofactors are classified into two groups: metals and small organic molecules (coenzymes).
- Prosthetic Group: A tightly bound cofactor essential for enzymatic function.
Vitamins as Coenzymes
- Water-soluble and selected fat-soluble vitamins function as cofactors or coenzymes.
- Coenzymes are crucial in energy release, catabolism, anabolic reactions, blood coagulation, and collagen integrity.
Water-Soluble Vitamins
- Vitamin B1 (Thiamine): Converted to thiamine pyrophosphate; aids in C-C bond cleavage through nucleophilic attack.
- Vitamin B2 (Riboflavin): Forms FMN and FAD; participates in redox reactions, accepting/donating electrons.
- Vitamin B6 (Pyridoxal): Converted to pyridoxal phosphate; forms Schiff bases facilitating various bond cleavages.
- Vitamin B12 (Cyanocobalamin): Acts in methyl group transfers; important in the synthesis of methionine.
Additional Water-Soluble Vitamins
- Nicotinamide (Niacin): Forms NAD/NADP; functions in redox reactions.
- Pantothenic Acid: Participates in activating acyl moieties for metabolic reactions.
- Biotin: Involved in carboxylation reactions, strongly binds to avidin.
- Vitamin C (Ascorbic Acid): Important for hydroxylation in collagen synthesis and potential immune support.
- Folic Acid: Converted to THF; carries C-1 groups; more of a substrate than coenzyme.
Lipid-Soluble Vitamins
- Vitamin A (Trans-retinol): Converted to cis-retinal; important for vision and growth.
- Vitamin D: Converted to hormone regulating calcium metabolism and gene expression.
- Vitamin E (a-Tocopherol): An antioxidant that aids in preventing sterility in animals.
- Vitamin K: Essential for blood coagulation and formation of calcium-binding proteins.
Non-Vitamin Coenzymes
- Lipoic Acid: Critical for electron/acetyl group transfer in the pyruvate dehydrogenase complex.
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Description
This quiz covers essential concepts related to amino acids, peptides, and proteins, focusing on their structures, properties, and functions. It also explores the classification of amino acids and their behavior as acids and bases. Perfect for students of Biochemistry.