a) A protein is found to be a tetramer of identical subunits. Name two symmetries 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 typesof subunits, α and β. What is the highest symmetry now possible?

a) A protein is found to be a tetramer of identical subunits. Name two symmetries 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 typesof subunits, α and β. What is the highest symmetry now possible?

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 24QP: a. Can a mutation change a proteins tertiary structure without changing its primary structure? b....

See similar textbooks

Similar questions

A protein is found to be a tetramer of identical subunits. Name two symmetries possible for such a molecule. What kinds of interactions (isologous or heterologous) would stabilize each?(a) Suppose a tetramer, like hemoglobin, consists of two each of two typesof subunits, α and β. What is the highest symmetry now possible?
Most proteins contain more than 100 amino acid residues. If you decided to synthesize a “100-mer,” with 20 different amino acids available for each position, how many different molecules could you make?
Our understanding of how proteins fold allows us to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence :a)Where might bends or βturns occur? b)Where might intrachain disulphide cross-linkages be formed? c)Assuming that this sequence is part of a bigger globular protein, indicate the probable location (on the surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln and Lys. Explain your reasoning
The interactions between the 2 a and 2 b subunits of hemoglobin represent what type of protein structure?
A protein contains three 60-kD polypeptides and six 20-kD polypeptides. Each 60-kD chain is disulfide bonded to two 20-kD chains. The 100-kD units associate noncovalently to form a protein with a molecular mass of 300 kD. Which of the following is correct? a) PAGE shows one single band b) Molecular masses determined by SDS-PAGE with 2-mercaptoethanol are 20kD and 60 kD c) Molecular mass determined by gel filtration is 300 kD d) All answers are correct e) Molecular mass determined by SDS-PAGE without 2-mercaptoethanol is 100 kD can you explain the steps and calculations to solve this question?
What two factors determine the primary structure of a polypeptidechain?
The common naturally occurring form of cysteine has a chirality center that is named (R), however; (a) What is the relationship between (R)-cysteine and (S)-alanine? (b) Do they have the opposite three-dimensional configuration (as the names might suggest) or the same configuration? (c) Is (R)-cysteine a D-amino acid or an L-amino acid?
In the illustration below, the blue squiggly line represents a protein. Notice that the amino acid that is colored red and the amino acid that is colored black are very close to each other in space, but they are far from each other in the primary structure of this protein. How can you explain why two amino acids that are so far from each other in the primary structure of a protein can be so close together in the tertiary structure of the same protein?
if glutamic acid were replaced by proline in a protein, how would the tertiary structure be affected?
Which R group would most likely be found in a hydrophobic area of the tertiary structure of a globular protein?
Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence.(a) Where might bends or β turns occur?(b) Where might intrachain disulfide cross-linkages be formed?(c) Assuming that this sequence is part of a larger globular protein, indicate the probable location (external surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln, Lys. Explain your reasoning.
An unspecified protein contains a 15-residue long α-helix with the following sequence: WEANIKQRLSTMGEYKQCHANG a. How many full turns are there in this α-helix? b. What is the length of the helix (in Angstroms) in the direction of the helix axis? c. How many hydrogen bonding interactions would be there in this α-helix? d. If it was a 310 helix instead with a helical pitch of 6 Å, is it long enough to span the 30 Å bilayer? Calculate and explain.