Xiong, K and Asciutto, EK and Madura, JD and Asher, SA
(2009)
Salt dependence of an α-helical peptide folding energy landscapes.
Biochemistry, 48 (45).
10818 - 10826.
ISSN 0006-2960
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Abstract
We used CD,UV resonance Raman spectroscopy, and molecular dynamics simulation to examine the impact of salts on the conformational equilibria and the Ramachandran Ψ angle (un)folding Gibbs free energy landscape coordinate of a mainly polyalanine α-helical peptide, AP of sequence AAAAA-(AAARA)3A. NaClO4 stabilizes α-helical-like conformations more than does NaCl, which stabilizes more than Na 2SO4 at identical ionic strengths. This α-helix stabilization ordering is the reverse of the Hofmeister series of anions in their ability to disorder water hydrogen bonding. Much of the NaClO4 α-helix stabilization results from ClO4- association with the AP terminal-NH3+ groups and Arg side chains. ClO4- stabilizes 310-helix conformations but destabilizes turn conformations. The decreased Cl- and SO 42- AP α-helix stabilization probably results from a decreased association with the Arg and terminal -NH3+ groups. Cl- is expected to have a smaller binding affinity and thus stabilizes α-helical conformations intermediately between NaClO 4 and Na2SO4. Electrostatic screening stabilizes π-bulge conformations. © 2009 American Chemical Society.
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Details
Item Type: |
Article
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Status: |
Published |
Creators/Authors: |
Creators | Email | Pitt Username | ORCID  |
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Xiong, K | | | | Asciutto, EK | | | | Madura, JD | | | | Asher, SA | asher@pitt.edu | ASHER | |
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Date: |
17 November 2009 |
Date Type: |
Publication |
Journal or Publication Title: |
Biochemistry |
Volume: |
48 |
Number: |
45 |
Page Range: |
10818 - 10826 |
DOI or Unique Handle: |
10.1021/bi9014709 |
Schools and Programs: |
Dietrich School of Arts and Sciences > Chemistry |
Refereed: |
Yes |
ISSN: |
0006-2960 |
MeSH Headings: |
Hydrogen Bonding; Peptides--chemistry; Protein Folding; Salts--chemistry; Spectrum Analysis--methods |
Other ID: |
NLM NIHMS207430, NLM PMC2952400 |
PubMed Central ID: |
PMC2952400 |
PubMed ID: |
19845367 |
Date Deposited: |
08 Feb 2013 20:49 |
Last Modified: |
22 Jun 2021 13:55 |
URI: |
http://d-scholarship.pitt.edu/id/eprint/17263 |
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