Xiong, K and Ma, L and Asher, SA
(2012)
Conformation of poly-L-glutamate is independent of ionic strength.
Biophysical Chemistry, 162.
1 - 5.
ISSN 0301-4622
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Abstract
CD and UV resonance Raman measurements surprisingly find that the charge screening of even 2 M concentrations of NaCl and KCl does not alter the unfolded PPII and 2.5 1-helix conformations of poly-l-glutamate. These salts appear to be excluded from the region between the side chain charges and the peptide backbone. Furthermore, no direct ion pairing occurs between these salts and the side chain carboxylates. © 2011 Elsevier B.V. All rights reserved.
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Details
Item Type: |
Article
|
Status: |
Published |
Creators/Authors: |
Creators | Email | Pitt Username | ORCID ![](/images/orcid_id_24x24.png) |
---|
Xiong, K | | | | Ma, L | | | | Asher, SA | asher@pitt.edu | ASHER | |
|
Date: |
1 March 2012 |
Date Type: |
Publication |
Journal or Publication Title: |
Biophysical Chemistry |
Volume: |
162 |
Page Range: |
1 - 5 |
DOI or Unique Handle: |
10.1016/j.bpc.2011.11.002 |
Schools and Programs: |
Dietrich School of Arts and Sciences > Chemistry |
Refereed: |
Yes |
ISSN: |
0301-4622 |
MeSH Headings: |
Circular Dichroism; Models, Molecular; Osmolar Concentration; Polyglutamic Acid--chemistry; Potassium Chloride--chemistry; Protein Structure, Secondary; Sodium Chloride--chemistry; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman |
Other ID: |
NLM NIHMS342684 [Available on 03/01/13], NLM PMC3288237 [Available on 03/01/13] |
PubMed Central ID: |
PMC3288237 |
PubMed ID: |
22236769 |
Date Deposited: |
14 Feb 2013 21:18 |
Last Modified: |
12 Jun 2021 23:55 |
URI: |
http://d-scholarship-dev.library.pitt.edu/id/eprint/17290 |
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