Title of article
Conformation of poly-l-glutamate is independent of ionic strength Original Research Article
Author/Authors
Kan Xiong، نويسنده , , Chun-Lu Ma، نويسنده , , Sanford A. Asher، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2012
Pages
5
From page
1
To page
5
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.
Keywords
Poly-l-glutamate , PPII , 2.51-Helix , Salt exclusion , UV resonance Raman
Journal title
Biophysical Chemistry
Serial Year
2012
Journal title
Biophysical Chemistry
Record number
1120547
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