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Questions and Answers
What is the primary bond responsible for holding two amino acids together?
What type of interactions are responsible for the tertiary structure of a protein?
What is the term for the process of disrupting the native structure of a protein?
What is the role of enzymes in biological reactions?
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What is the term for short chains of amino acids containing fewer than 50 amino acids?
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What is the level of protein structure that is dependent on the tertiary structure of individual polypeptides?
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What is the role of the four calcium ions in thermolysin?
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Which type of amino acid residues are resistant to heat cleavage by trypsin and chymotrypsin?
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What is the function of CNBr in protein chemistry?
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What is the purpose of hydrazinolysis in protein chemistry?
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What is the primary structural component of all tissues in humans and other animals?
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What are proteins composed of?
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What is the term for the region of the enzyme molecule where the substrate binds?
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What is the term for the substance that an enzyme acts on in a reaction?
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What is the term for an enzyme without its non-protein moiety?
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What type of cofactor is loosely bound to an enzyme by non-covalent bonds?
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What is the term for the complex formed when a substrate binds to an enzyme?
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What type of cofactor is tightly bound to an enzyme by covalent bonds?
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What is the primary function of gel electrophoresis in protein analysis?
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Which reagent reacts with the N-terminus of an amino acid?
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What is the specific function of trypsin in proteolytic cleavage?
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What is the purpose of using papaya (papain) in meat tenderization?
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Which of the following is NOT a function of chymotrypsin?
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What is the reaction mechanism of Dansyl chloride with amino acids?
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What is the biochemical activity of the enzyme catalase?
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Which type of enzyme catalyses the reaction of joining two molecules with covalent bonds using energy from ATP?
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What is the biochemical activity of transaminases such as ALT and AST?
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Which of the following enzymes is an example of a phosphotransferase?
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What is the biochemical activity of the enzyme phenylalanine hydroxylase?
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Which of the following enzymes is an example of a lyase?
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Study Notes
Amino Acids and Proteins
- There are 20 different types of amino acids that constitute the monomer units of proteins.
- Amino acids are linked together by peptide bonds to form chains, which can be classified as peptides (short chains, fewer than 50 amino acids) or polypeptides (longer chains).
- Each protein has its own unique combination of amino acids.
Protein Structure
- Proteins have unique shapes due to bonding arrangements, including:
- Peptide bonds (primary)
- Hydrogen bonding (secondary and tertiary)
- Ionic attraction/bonds (tertiary)
- Hydrophobic and hydrophilic interactions (tertiary)
- Covalent sulfur bonds (tertiary)
- Quaternary structure is dependent on the tertiary structure of individual polypeptides and is influenced by these bonds.
Protein Denaturation
- Proteins can be denatured by:
- Heat
- Mechanical agitation
- Detergents
- Organic compounds
- pH changes
- Inorganic salts
Enzymes
- Enzymes are proteins that increase the rate of reaction by lowering the energy of activation.
- They catalyze nearly all chemical reactions in the body's cells.
- Enzymes are not altered or consumed during reaction.
- Example: Thermolysin, a thermostable zinc endopeptidase, contains zinc and four calcium ions necessary for its thermal stability.
Enzyme Structure and Function
- The active site is the area on the enzyme where the substrate or substrates attach.
- Enzymes contain a special pocket or cleft called the active site.
- Apoenzyme is an inactive enzyme without its non-protein moiety, while holoenzyme is an active enzyme with its non-protein component.
- Cofactors are non-protein chemical compounds bound to an enzyme, required for catalysis.
- Types of cofactors include coenzymes and prosthetic groups.
Enzymatic Reactions
- Substrate is the substance at the beginning of the enzymatic reaction.
- Enzyme-substrate complex forms when the substrate binds to the enzyme.
- Examples of enzymes include lactate dehydrogenase, glucose oxidase, and peroxidase.
Biochemical Activity
- Transferases: transfer functional groups between donor and acceptor molecules.
- Hydrolases: catalyze the hydrolysis of various bonds.
- Lyases: cleave various bonds by means other than hydrolysis and oxidation.
- Isomerases: catalyze isomerization changes within a single molecule.
- Ligases: join two molecules with covalent bonds using energy from ATP.
Chemical Methods
- Proteolytic enzymes: cleave polypeptides into smaller fragments.
- Cyanogen bromide (CNBr): cleaves at methionine residues.
- Dansyl chloride: reacts with primary amino groups to produce stable blue- or blue-green-fluorescent sulfonamide adducts.
- Other chemical methods: BNPS-skatole, formic acid, hydroxylamine, and 2-nitro-5-thiocyanobenzoic acid (NTCB).
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Description
This quiz covers various techniques used in protein analysis, including enzymatic cleavage, gel electrophoresis, and Dansyl Chloride. Learn how to break down polypeptides into smaller fragments and analyze them using these methods. A great resource for biochemistry and molecular biology students!
