. Apamine is a small protein toxin present in the venom of the honeybee. Ithas the sequenceCNCKAPETALCARRCQQH(a) If apamine does not react with iodoacetate (see Tools of Biochemistry5B), then how many disulfide bonds are present?(b) If trypsin cleavage gave two peptides, then where is(are) the S-Sbond(s)?

Apamin is an 18-residue bee venom peptide with the sequence CNCKAPETALCARRCQQH-amide. It is an 18…

Answered: . Apamine is a small protein toxin…

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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Macmillan Learning Consider the structure of methionine in its +1 charge state. H₂N CH₂ CH₂ CH3 -OH Give the pK, value for the a-amino group of methionine. An answer within ±0.5 units is acceptable. Give the pK, value for the a-carboxyl group of methionine. An answer within +0.5 units is acceptable. Determine the isoelectric point (pl) for methionine. Give your answer to two decimal places. pK (−NH ) = pK₂ (-COOH) = pl = 5.74 2.28 Incorrect 9.21 Incorrect Attempt
Draw the chair conformation of the whole of O-linked oligosaccharide pictured below, including the amino acid it is attached to.
Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.
Activity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1. Glycyl-valyl-serine 2. Threonyl-cysteine 3. Isoleucyl-methionyl-aspartate
This image is showing the conformations of ubiquitin superimposed. What do the structures in this figure tell us about the dynamics of enzymes? Discuss the limitations of crystal structures in the analysis of proteins. What are the benefits? What are the advantages of NMR structures?
Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.
(A) Give the polypeptide translation of the RNA sequence below. 5’-AUGGAAAUCAAAGUCAACCUUGAGUUUAGA-3’ (B) Write the chemical structure of the polypeptide sequence you determined in part (a) (C) Given the chemical structure of the polypeptide sequence you have written in part (b), answer True or False for each of the 5 statements below. (1) At least one of the amino acids in the sequence can undergo phosphorylation (2) The sequence looks like it could form a β turn (3) The sequence looks like it could form a β strand with one surface facing the interior of the protein and the other surface exposed to water (4) At least one of the amino acids in the polypeptide sequence can undergo oxidation to form a disulfide bridge to another polypeptide (5) The sequence looks like it could form an α helix that would be part of a coiled coil structure within a protein
25) Below are two amino acids: cysteine and histidine. a) Draw the reaction mechanism of a dehydration synthesis reaction between cysteine and histidine below: HS H Product 1 OH ox HN H b) Draw two different products of the dehydration synthesis reaction from part a). Prove that these are two different products by labelling the N and C termini, peptide bond, and R-groups of each product. Product 2 OH
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