(a) A protein is found to be a tetramer of identical subunits. Name twosymmetries possible for such a molecule. What kinds of interactions (isologous or heterologous) would stabilize each?(b) Suppose a tetramer, like hemoglobin, consists of two each of two types ofsubunits, a and B. What is the highest symmetry now possible?

Tetramer : It is an oligomer formed from four monomers or subunits. The associated property is…

Answered: (a) A protein is found to be a tetramer…

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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Similar questions

The variable structures of a nucleotide are the sugar and the phosphate group. (a). Say if the statement written above is true or false. (b). Give ONE reason for your answer in part (a).
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.
Within a naturally-occurring polypeptide, under neutral pH conditions (pH = 7.0), which of the following amino acids always has a negatively charged carboxyl group? the first amino acid in the primary structure histidine lysine arginine the last amino acid in the primary structure
(b) The structure of a drug called tirbanibulin which is used to treat a pre-cancerous skin condition called actinic keratosis is shown below. (i) (ii) (iii) (iv) ہے مههممنن State Lipinski's Rule of Five (ROF) and Veber's addition to the ROF. Briefly state why the ROF is used in medicinal chemistry?. Given that the molecular mass of tirbanibulin is 431.536 g.mol-¹ and its log P is 3.2, apply the ROF and Veber's additional rule to this drug and show clearly how you arrived at your answer. Comment on the outcome of your analysis of the structure in part (iii).
Regarding the last answer choice, how come both alpha helices and beta sheets aren't denatured when the heat breaks peptide bonds? If heat were to break peptide bonds, wouldn't that affect the primary structure which inevitably affects the more complicated structures?
Assume you were given a mixture consisting of one molecule each of all possible sequences of a smallish protein of molecular weight 4800 daltons. If the average molecular weight of an amino acid is, say, 120 daltons, how much would the sample weigh? How big a container would you need to hold it?
(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
The following illustrations show examples of the secondary, supersecondary (motifs), tertiary or quaternary structures, as we discussed. Select the most appropriate illustration marked "A-E. Greek key motif: A E OA. A OB. B OC.C O D.D OE. E

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