relation: http://d-scholarship-dev.library.pitt.edu/17290/
title: Conformation of poly-L-glutamate is independent of ionic strength
creator: Xiong, K
creator: Ma, L
creator: Asher, SA
description: 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.
date: 2012-03-01
type: Article
type: PeerReviewed
format: text/plain
language: en
rights: attached
identifier: http://d-scholarship-dev.library.pitt.edu/17290/1/licence.txt
identifier:   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     
relation: 10.1016/j.bpc.2011.11.002