Michaelis menten kinetics - Study guides, Class notes & Summaries

LECTURE 7 PSCI EXAM REVIEW QUESTIONS AND ANSWERS, RATED A+ Drug transporters follow what kinetics Michaelis-Menten Enzyme Kinetics Vmax maximum velocity Km Substrate concentration at 1/2 Vmax Types of inhibitors competitive and non-competitiv

Tri 1 Biochem Past Exams Questions and Answers Already Passed What is the role of zinc in enzyme function? Zinc acts as a cofactor, stabilizing the structure of enzymes and aiding in catalysis. Which type of bond forms between the amino group of one amino acid and the carboxyl group of another? A peptide bond forms between the amino and carboxyl groups, linking amino acids together. How do enzymes use the lock-and-key model to explain substrate binding? The lock-and-key model ...

MCAT Bio/Biochem Questions and Answers | Latest Version | 2024/2025 | 100% Verified Explain the role of the sodium-potassium pump in maintaining resting membrane potential. The sodium-potassium pump actively transports three sodium ions out of the cell and two potassium ions into the cell, helping to maintain the resting membrane potential by creating an electrochemical gradient. Describe the process of oxidative phosphorylation in cellular respiration. Oxidative phosphorylatio...

Pre-PCOA Exam Latest Update (2022/2023) Already Passed Methods to enhance a drug's solubility in a solvent 1. Heat 2. Co-solvents increase the solubility of hydrophobic molecules by reducing the dielectric constant of the solvent 3. pH-Assisted solubility processes of drug elimination from the body liver, kidney and bile primary, secondary, tertiary and quaternary structures of proteins a. 1° primary - amino acid sequence of the polypeptide (Controls levels 2, 3, and 4) b. 2° secondary - l...

First Aid USMLE Step 1: Pharmacology 2023 In the Michaelis-Menten kinetics what do the following mean: Km Vmax Draw a typical hyperbolic curve on a Michaelis-Menten Plot, then draw how the addition of a competitive and non-competitive inhibitor would change the kinetics of the reaction. - ANS-*In the Michaelis-Menten kinetics what do the following mean:* Km: - the concentration of substrate at 1/2 Vmax - this is INVERSELY related to the affinity of enzyme for its substrate Vmax: ...

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...

If the pka of a weak acid is 2.5, at which pH will this drug become more ionized? A. pH 5 B. pH 2.5 C. pH 1.5 D. pH 1 - Answer - A. For a weak acid, a higher pH increases ionization Which equation describes the rate of drug dissolution from a tablet? A. Fick's Law B. Henderson-Hasselbalch equation C. Michaelis-Menten equation D. Noyes-Whitney equation - Answer - D. The Noyes-Whitney equation describes the rate of drug dissolution from a tablet. Fick's first law of diffusion is s...

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...

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

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 ...