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Conformation of poly-L-glutamate is independent of ionic strength

UNSPECIFIED (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 2.51-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
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: 05 Jan 2019 15:59
URI: http://d-scholarship.pitt.edu/id/eprint/17290

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