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UV resonance Raman studies of the NaClO<inf>4</inf>dependence of poly-l-lysine Conformation and hydrogen exchange kinetics

UNSPECIFIED (2012) UV resonance Raman studies of the NaClO<inf>4</inf>dependence of poly-l-lysine Conformation and hydrogen exchange kinetics. Journal of Physical Chemistry B, 116 (3). 1134 - 1142. ISSN 1520-6106

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Abstract

We used 204 nm excitation UV Resonance Raman (UVRR) spectroscopy to examine the effects of NaClO4on the conformation of poly-l-lysine (PLL). The presence of NaClO4induces the formation of α-helix, π-helix/bulge, and turn conformations. The dependence of the AmIII3frequency on the peptide ψ Ramachandran angle allows us to experimentally determine the conformational population distributions and the energy landscape of PLL along the Ramachandran ψ angle. We also used UVRR to measure the NaClO4concentration dependence of PLL amide hydrogen exchange kinetics. Exchange rates were determined by fitting the D2O exchanging PLL UVRR AmII′ band time evolution. Hydrogen exchange is slowed at high NaClO4concentrations. The PLL AmII′ band exchange kinetics at 0.0, 0.2, and 0.35 M NaClO4can be fit by single exponentials, but the AmII′ band kinetics of PLL at 0.8 M NaClO4requires a double exponential fit. The exchange rates for the extended conformations were monitored by measuring the Cα-H band kinetics. These kinetics are identical to those of the AmII′ band until 0.8 M NaClO4whereupon the extended conformation exchange becomes clearly faster than that of the α-helix-like conformations. Our results indicate that ClO4-binds to the PLL backbone to protect it from OH-exchange catalysis. In addition, ClO4-binding also slows the conformational exchange between the extended and α-helix-like conformations, probably by increasing the activation barriers for conformational interchanges. © 2011 American Chemical Society.


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Details

Item Type: Article
Status: Published
Date: 26 January 2012
Date Type: Publication
Journal or Publication Title: Journal of Physical Chemistry B
Volume: 116
Number: 3
Page Range: 1134 - 1142
DOI or Unique Handle: 10.1021/jp208918n
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 1520-6106
MeSH Headings: Amides--chemistry; Chlorates--chemistry; Hydrogen--chemistry; Hydrogen-Ion Concentration; Kinetics; Peptides--chemistry; Polylysine--chemistry; Protein Folding; Protein Structure, Secondary; Spectrum Analysis, Raman--methods
Other ID: NLM NIHMS345463, NLM PMC3266997
PubMed Central ID: PMC3266997
PubMed ID: 22117822
Date Deposited: 08 Feb 2013 20:47
Last Modified: 05 Jan 2019 15:59
URI: http://d-scholarship.pitt.edu/id/eprint/17281

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