Michaelis menten - Study guides, Class notes & Summaries

Michaelis-Menten Kinetics Correct Answer [S] = Concentration of substrate V = Velocity Km is inversely related to the affinity of the enzyme for its substrate Vmax = Directly proportion to the enzyme concentration Most enzymatic reactions follow of hyperbolic curve [Michaelis-Menten] kinetics Enzymatic reactions that exhibit a sigmoid curve [Hemoglobin] exhibit positive cooperativity Lineweaver-Burk Correct Answer ↑ y-intercept, ↓ Vmax The further to the right, the x-intercept [Cl...

Biochemistry Test 1 Questions and Answers Graded A+ What is the role of allosteric sites in enzyme regulation? Allosteric sites are regions where molecules can bind and influence enzyme activity by changing its shape. How do competitive inhibitors affect enzyme function? Competitive inhibitors compete with substrates for binding at the active site, reducing enzyme activity. What determines the tertiary structure of a protein? The tertiary structure is determined by interactio...

structures and properties of amino acids Nonpolar, Aliphatic (Hydrophobic): Glycine (Gly, G) Alanine (Ala, A) Valine (Val, V) Leucine (Leu, L) Isoleucine (Ile, I) Proline (Pro, P) Aromatic (Hydrophobic): Phenylalanine (Phe, F) Tyrosine (Tyr, Y) Tryptophan (Trp, W) Polar, Uncharged (Hydrophilic): Serine (Ser, S) Threonine (Thr, T) Cysteine (Cys, C) Methionine (Met, M) Asparagine (Asn, N) Glutamine (Gln, Q) Positively Charged (Basic, Hydrophilic): Lysine (Lys, K) Arginin...

USMLE Step 1 Pharmacology Verified Solutions 2023 Michaelis-Menten Kinetics - ANS-[S] = Concentration of substrate V = Velocity Km is inversely related to the affinity of the enzyme for its substrate Vmax = Directly proportion to the enzyme concentration

tbr- enzyme kinetics exam questions & answers 2024 allosteric enzyme - ANSWER-often have multiple inhibitor or activator binding sites to change conformation, switching between active and inactive shapes allosteric curve - ANSWER-sigmoidal shape ex. hemoglobin = allosteric protein transition state analogs - ANSWER-synthesized compounds that mimic the form of the transition state of a substrate molecule and binds to the enzyme to inhibit catalysis rxn transition state vs intermedi...

An α-helical arrangement of amino acids is considered to be what level of protein structure? correct answer: Secondary structure of the protein β- sheets and α-helices are examples of secondary structures. How these structures interact would be an example of tertiary structure. If a mutation is made within the active site of an enzyme resulting in a decrease in Km, which of the following will be true with respect to the enzyme kinetics? correct answer: The enzyme will require a lower ...

Which of the following interactions are generally considered to be unfavorable? - Interaction between Arg and Lys side chains at a pH of 7, assuming standard pKa values for Arg and Lys Proteins can be denatured by a) Changing temperature b) Adding urea to solution c) Changing solvent d) all choices are correct - All choices are correct If PAGE is carried out after subjecting the sample to SDS and beta-mercaptoethanol, then proteins will be separated on the basis of - Mass Which is the most...

UNE Biochem 1005 Final Study Set Questions With Complete Solutions. Which of the following best describes the structure of heme? -a nicotinamide structure that is readily oxidized -a negatively charged phosphate group -a planar porphyrin ring that binds iron -an n-link glycosylation A planar porphyrin ring that binds iron Covalent catalysis is used by many enzymes to cleave peptide bonds. Which of the following amino acids would not facilitate this type of catalysis? -valine -cystei...

A complex organic molecule that is necessary for enzyme function but is NOT permanently associated with the enzyme is a: A) prosthetic group. B) cofactor. C) holofactor. D) coenzyme. E) metal ion. - D) coenzyme. A double-reciprocal plot of 1/V0 versus 1/[S] for an enzyme in the presence of increasing concentrations of an uncompetitive inhibitor will have lines corresponding to the different inhibitor concentrations that are BEST described by which statement? A) The lines will intersect...

UNE Biochem 1005 Final Study Set Questions With Complete Solutions. Which of the following best describes the structure of heme? -a nicotinamide structure that is readily oxidized -a negatively charged phosphate group -a planar porphyrin ring that binds iron -an n-link glycosylation A planar porphyrin ring that binds iron Covalent catalysis is used by many enzymes to cleave peptide bonds. Which of the following amino acids would not facilitate this type of catalysis? -valine -cystei...