Which of the following statements are descriptions of metal ion catalysis orexamples of metal ion catalysis? Choose all correct answersa Zn²+ cofactor may properly orient the substrate in the active site throughionic interactions.a covalent bond forms between enzyme and substratelowers the energy or stabilizes the transition state or intermediatecatalyst retains its original form after reaction occurscatalysts may participate in oxidation-reduction reactions by changes in theoxidation state Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equalto the pK value for the free amino acid in solution.)histidineleucineaspartic acidlysine

Introduction: Nearly one-third of all known enzymes require metal ions for the catalytic activity…

Answered: Which of the following amino acid…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Trypsin contains a/an [aspartate/serine/histidine] in its specificity pocket to attract lysine and arginine side chains. It contains a potent nucleophilic [histidine/serine/aspartate] in its active site that is capable of attacking the electrophilic [carbon/nitrogen/oxygen] of the closest peptide bond. The [acyl-enzyme/specificity pocket/oxyanion] transition state is stabilized by the backbone amide hydrogens of glycine and serine. In this way, the enzyme is able to catalyze the [hydrolysis/ligation/metalysis/hydrogenation] of the peptide bond.
When performing his experiments on protein refolding, Christian Anfinsen obtained a quite different result when reduced ribonuclease was reoxidized while it was still in 8 M urea and the preparation was then dialyzed to remove the urea. Ribonuclease reoxidized in this way had only 1% of the enzymatic activity of the native protein. Why were the outcomes so different when reduced ribonuclease was reoxidized in the presence and absence of urea?
Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein. please do not copy from other answers here
PLP is a cofactor for a number of enzymes involved in amino acid metabolism. Give an example of reaction in which PLP participates in cleavage of the a, b, and c bonds of an amino acid, as diagrammed in shown Fig.
Consider a hexapeptide of the sequence thr asn glu trp lys gln. After complete hydrolysis, which amino acid would elute first from a cation exchange column at pH 7? O Asn O GIn Thr Glu O Trp O Lys
Is a protein as good a cellular buffer at physiological pH as its constituent amino acids would be if they were present as free amino acids in proportional concentrations in the cell? Explain Based on your rationale in the previous question, describe the difference in the dissociation constants of the α-COOH of GABA and glutamate, and the differences in the dissociation constants of the amino group in each of these amino acids.
Sketch the following two tripeptide chains: Asp-Gly-Ser and Ile-Asn-Met at physiological pH . Please provide only typed answer solution no handwritten solution needed allowed
The molecular iodine (12) in betadine is susceptible to decomposition if exposed to direct sunlight, which lowers the concentration of 12 solution. After performing the standardization step in home experiment 9, a student leaves their betadine solution in direct sunlight for several hours before coming back to perform the titration of ascorbic acid in orange juice. Assuming that the concentration of 12 is reduced by the sunlight, how would this affect the measured value of the concentration of ascorbic acid in the orange juice? The measured concentration of ascorbic acid would be higher The measured concentration of ascorbic acid would be lower There is not enough information to determine the affect on the measured concentration of ascorbic acid The measured concentration of ascorbic acid would be unaffected
Equilibrium constants are always dependent upon temperature. In determining equilibrium constants for biochemical reactions the equilibrium constant also depends upon ion concentration and proton concentration. Write down an equation in differential form that describe the dependence of an equilibrium constant K for a protein binding to DNA, where the equilibrium constant, K is a function of Temperature, [NaCI], and [H*], i.e. dK(T, [NaCl], [H*]).
A seven-residue peptide was found to have an amino acid composition including glu, val, Lys, met, leu, and trp (there is more than one copy of one amino acid). Several reactions on samples of the peptide resulted in the following: a) Trypsin has no effect on the heptapeptide. b) If one cycle of Edman degradation provides the PTH derivative shown below, what does this tell you about the oligopeptide under investigation? [image] c) Chymotrypsin treatment yields a dipeptide, a tetrapeptide, and a free amino acid. Possibilities? d) The tetrapeptide contains val, lys, and met (only). What information does this give you? e) Cyanogen bromide treatment generates a dipeptide, a tetrapeptide, and free Lys. f)What is the sequence of the peptide?
Intramitochondrial ATP concentrations are about 5 mM, and phos- phate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentra- tion of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
Heparin, a highly negatively charged glycosaminoglycan, is used clinically as an anticoagulant. It acts by binding several plasma proteins, including antithrombin III, an inhibitor of blood clotting. The 1:1 binding of heparin to antithrombin III seems to cause a conformational change in the protein thatgreatly increases its ability to inhibit clotting. What amino acid residues of antithrombin III are likely to interact with heparin?

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Which of the following amino acid residues would not provide a side chain for acid- base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) histidine leucine aspartic acid lysine