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Raman studies of solution polyglycine conformations

Bykov, S and Asher, S (2010) Raman studies of solution polyglycine conformations. Journal of Physical Chemistry B, 114 (19). 6636 - 6641. ISSN 1520-6106

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Polyglycine (polygly) is an important model system for understanding the structural preferences of unfolded polypeptides in solution. We utilized UV resonance and visible Raman spectroscopy to investigate the conformational preferences of polygly peptides of different lengths in water containing LiCl and LiClO4. Lithium salts increase the solubility of polygly. Our study indicates that in solution the conformational ensemble of polygly, as well as central peptide bonds of gly5 and gly6, are dominated by the 31 extended helix, also known as the polyglycine II conformation (PGII). This preference of the polygly backbone for the PGII conformation in solution is likely a result of favorable interactions between carbonyl dipoles in these extended helices. We found that high concentrations of Li+ stabilize the PGII conformation in solution, most likely by polarizing the peptide bond carbonyls that makes PGII-stabilizing carbonyl-carbonyl electrostatic interactions more favorable. This ability of Li+ to stabilize 31-helix conformations in solution gives use to the denaturing ability of lithium salts. © 2010 American Chemical Society.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Bykov, S
Asher, Sasher@pitt.eduASHER
Date: 20 May 2010
Date Type: Publication
Journal or Publication Title: Journal of Physical Chemistry B
Volume: 114
Number: 19
Page Range: 6636 - 6641
DOI or Unique Handle: 10.1021/jp100082n
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 1520-6106
MeSH Headings: Lithium Chloride--chemistry; Peptides--chemistry; Protein Structure, Secondary; Solutions; Spectrum Analysis, Raman
Other ID: NLM NIHMS199672, NLM PMC2879021
PubMed Central ID: PMC2879021
PubMed ID: 20415491
Date Deposited: 08 Feb 2013 20:55
Last Modified: 22 Jun 2021 13:55


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