Lysozyme cleaves between NAG and NAM residues in bacterial cell walls and is, therefore, classified as a(an) O A. salt bridge, oxidoreductase B. peptide bond; hydrolase OC. glycosidic linkage; oxidoreductase O D. glycosidic linkage; hydrolase O E. peptide bond; transferase
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- mutate all of your D-form amino acids in your peptidoglycan peptide side chains to L forms. What have just done to your peptidoglycan? • A. You prevent lysozyme from being able to work • B. You prevent NAM and NAG from linking together C. You have made it susceptible to degradation by proteases • D. You prevent it from being flipped from the cytoplasm across the plasma membrane O E. Nothing, there is no difference between the L and D forms of amino acidsOrganisms (like mice) that contain essential selenoproteins_____ Select one: a. posses tRNAs that bind to the amino acid selenocysteine b. posses scaffold proteins that bind to the cofactor selenocysteine c. acquire selenium from the atmosphere d. posses selenium fixation enzymes e. posses unique ribosomes that only make selenoproteins from selenocysteineTissues that are unable to produce nucleotides de novo depend on ____________________ to maintain an adequate supply of adenine nucleotides. (A) the redox reactions carried out by ribonucleotide reductase (B) the action of PRPP amidotransferase(C) uptake of ATP through dietary intake(D) salvaging hypoxanthine using HGPRT (E) the action of xanthine oxidase
- What impact do mutations in the alpha-chain usually have, if any, on hemoglobin's function? A. T-to-R-state transition B. dimer-dimer stabilization C. Allosteric Regulation D. A & B E. A & C F. A,B, & CExplain why lysozyme cleaves the artifi cial substrate (NAG)4 ~4000 times more slowly than it cleaves (NAG)6.You are studying how your Lys-Val-Thr tripep de interacts with another pep de, which places an Asp in close proximity to the Lys on your pep de. How would the presence of an Asp side chain affect the pKa of the Lys side chain? Briefly explain your reasoning. (remember pKas are rela ve, pKa=log([H+][A-]/[HA])
- Identify the following by describing their functions: EF-G, EF-Tu, EF-Ts, EF-P, and peptidyl transferaseIn PLP dependent enzymes, what amino acid is initially bound to PLP in the PLP-Schiff base state? a) Asparagine b) Lysine c) Glutamine d) ArginineElectrophoresis is performed at PH 6.8 on a mixture of mutated hemoglobin that differ from normal haemoglobin (Hb) only by the substitution of one amino acid- Hb X: Val replaced par Glu - Hb Y: Asp replaced by Leu - Hb Z: Glu replaced by Lys What will be the order of migration between cathode and anode of these mutated Hb compared to normal Hb? Justify your answer.
- The ESI-MS spectrum in positive ionization mode for lysozyme is obtained. a. What is the molecular weight of the protein to 5 significant figures based on the two highlighted ion species? b. What is the charge of the peaks at 1101.5 and 1789.2.The idea that primary sequence determines tertiary structure first came from experiments in the 1950's about: A. the renaturation of RNaseA (ribonuclease A). B. the denaturation of lysozyme. C. the 3D structure of lysozyme. D. the role of Hsp70 in protein folding. E. the role of PDI (protein disulfide isomerase) in protein folding.Explain what the meaning of these distances is (e.g., from where to where?)Crystal structure of human monocyte chemotactic protein-2