Lineweaver burk plot - Study guides, Class notes & Summaries

(T/F) Acid-base catalysis involving free protons or hydroxide ions is thermodynamically favorable because these are already in high concentrations in the cell. Correct Answer-False (T/F) The glycerophosopholipids of a membrane bilayer have been modified to contain additional double bonds. This change will likely lower the activation of adenylate cyclase by a G-protein. Correct Answer-False (T/F) To be inserted, a α-helical integral membrane protein requires at least one helix that is at l...

Dr Rai biochem test 2 questions & answers 2023/2024 kinetic mechanism - ANSWER-the order of binding of substrates and release of products sequential mechanism - ANSWER-each substrate binds but both substrates must be bound by enzyme to form a ternary complex before catalysis can occur ping pong mechanism (double displacement) - ANSWER-Substrate binds to the enzyme and releases a product before the second substrate binds to the enzyme Random order enzyme mechanism - ANSWER-any react...

diffusion controlled limit - Answer The theoretical maximum rate of an enzymatic reaction in solution, about 10^8 to 10^9 M^-1 * s^-1 catalytic perfection - Answer A state achieved by an enzyme that operates at the diffusion-controlled limit. Lineweaver-Burk plot - Answer A rearrangement of the michaelis menton equation that permits the determination of KM and Vmax from a linear plot.

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...

Biology 3221A Biochemistry Final Exam Q&A- Rush University Which of the following single-base DNA gene coding changes is least likely to significantly affect the function of resulting protein? (Harper pages 361-363) A. Missence mutation resulting to histidine-to-glutamic acid change B. Silent mutations in the third codon base C. Frameshift mutation D. Nonsense mutation 2. Which of the following is a property of enhancer elements? (Harper pages 384-385) A. They do not work located downs...

test_bank_for_biochemistry_8th_edition_by_berg_ibsn_9781464126109.Chapter 2 Protein Composition and Structure 1) Which of the following is most often found in proteins? A) D-amino acids B) L-amino acids C) an equal amount of D- and L-amino acids D) amino acids with the -carbon exclusively having an R absolute configuration E) amino acids with the -carbon exclusively having an S absolute configuration Answer: B Section: 2.1 2) A term that describes a molecule that contains both pos...

NBME Pharmacology Exam With 100% Correct And Verified Answers

Biochemistry Final Exam Practice 63 Questions with Verified Answers The central dogma of molecular biology teaches us that: a. RNA replicates itself and DNA is translated into protein b. RNA is typically the genetic material c. RNA contains information, which is translated into amino acid sequences d. Proteins are not needed to replicate DNA or transcribe RNA e. RNA is made of the same monomers as DNA - CORRECT ANSWER c. RNA contains information, which is translated into amino acid sequ...

what is Km - ANSWER-concentration of substrate at 1/2 Vmax what is Km inversely related to - ANSWER-the affinity of the enzyme for its substrate (low Km=high affinity & high Km=low affinity) what is Vmax directly proportional to - ANSWER-enzyme concentration most enzymes follow what kind of kinetics - ANSWER-Michaelis-Menten kinetics (line up and then it flattens out, hyperbolic) if an enzymatic rxn shows a sigmoid curve what does that indicate - ANSWERcooperative kinetics (hemoglobin) do...

Define Km in MM kinetics: - ANSWER-The concentration of substrate [S] at which 1/2 Vmax is reached Km is _________ related to affinity of the enzyme for its substrate - ANSWER-inversely Vmax is directly proportional to what? - ANSWER-to the enzyme concentration What characterizes MM kinetics? - ANSWER-a hyperbolic curve when Vmax is plotted against [S]. Most enzymes follow MM kinetics. Enzymatic reactions demonstrated a sigmoid curve usually denote: - ANSWERcooperative binding / kinetics, ...