Do you expect a Pro → Gly mutation in a surface-loop region of a globularprotein to be stabilizing or destabilizing? Assume the mutant folds to anative-like conformation. Explain your answer in terms of the predictedenthalpic and entropic effects of the mutation on the AG for protein foldingcompared to AG of folding for the wild-type protein.

Mutation : It is an alteration in the nucleotide sequence of the genome of an organism, virus, or…

Answered: Do you expect a Pro → Gly mutation in a…

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

See similar textbooks

Similar questions

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])
help
In a 0.1 M lysine solution, what are the individual concentrations of the protonated C-terminus form of the amino acid versus the non- protonated at pH 4 (pKa = 2.16)
Do you expect a Pro → Gly mutation in a surface-loop region of a globular protein to be stabilizing or destabilizing? Assume the mutant folds toa native-like conformation. Explain your answer in terms of the predictedenthalpic and entropic effects of the mutation on the ∆G for protein foldingcompared to ∆G of folding for the wild-type protein
In the fungus Neurospora, some mutants were obtainedthat lacked activity for a certain enzyme. The mutationswere found, by mapping, to be in either of two unlinkedgenes. Provide a possible explanation in reference to quaternary protein structure
The folding and unfolding rate constants for a myoglobin mutant have been determined. The unfolding rate constant ke-u = 3.62 x 10-55 and the folding rate constant ku-p = 255 s1, where Fis the folded protein and U is the unfolded (denatured) protein. For wild-type myoglobin, AG;u = +37.4 kJ/mol. Which myoglobin is more thermodynamically stable, the mutant or the wild-type?
The amide hydrogen atoms of peptide bonds within proteins can exchange with protons in the solvent. In general, amide hydrogen atoms in buried regions of proteins and protein complexes exchange more slowly than those on the solvent-accessible surface do. Determination of these rates can be used to explore the proteinfolding reaction, probe the tertiary structure of proteins, and identify the regions of protein–protein interfaces. These exchange reactions can be followed by studying the behavior of the protein in solvent that has been labeled with deuterium ( ²H), a stable isotope of hydrogen. What two methods described in this chapter could be readily applied to the study of hydrogen– deuterium exchange rates in proteins?
Consider the phenolic hydroxyl group of a particular Tyr residue in a protein. Suppose the hydroxyl group in the unfolded protein in aqueous solution, where the group is exposed to H2O, has a pKa of 10.0. If that group is found in a hydrophobic environment in the interior of the protein when the protein is folded into its native tertiary structure, would you expect the pKa of the phenolic hydroxyl to be higher or lower in the folded protein interior than in H2O? Explain your reasoning.
Briefly explain why a "Folding Funnel" is used to represent the kinetics of folding (limit 5-6 sentences)?
The trypsin enzyme is able to hydrolyze a peptide substate at the carboxyl side of an Arg or Lys residue. However, such a reaction can be also influenced by the amino acid residue that follows Arg or Lys. Given the Michaelis-Menton plots obtained for two substrates (substrate A: Ser-Val- Arg-Pro; substrate B: Ser-Val-Arg-Phe), the Km of the enzyme is higher for: 20 Substrate A Assume that these curves do not reach the same limit. 15 Substrate E 0.001 0.002 0.003 (Substrate) (molar) Inconclusive Substrate B Both Substrate A and B Intitial velocity (micromoles/literisecond)
Some of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a side chain for acid-base catalysis at physiological pH (assume pK of each amino acid is equal to pK value for the free amino acid in solution). Explain for each amino acid how and why each would or would not provide the side chain residue to support acid-base catalysis at physiological pH.
Sickle-cell disease is caused by a so-called point mutation in the humanβ - globin gene. A point mutation is the result of a single base substitution inthe DNA encoding a gene. The sickle-cell mutation results in the substitutionof Val for Glu at position 6 in the β - globin protein.(a) Using the information in as shown, explain how a point mutationcould change a codon for Glu to a codon for Val.(b) Do you expect the pI for the sickle-cell β - globin to be higher or lowerthan the pI for wild-type β-globin ? Explain.

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS