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UV resonance Raman determination of polyproline II, extended 2.5 <inf>1</inf>-helix, and β-sheet ψ angle energy landscape in poly-L-lysine and poly-L-glutamic acid

Mikhonin, AV and Myshakina, NS and Bykov, SV and Asher, SA (2005) UV resonance Raman determination of polyproline II, extended 2.5 <inf>1</inf>-helix, and β-sheet ψ angle energy landscape in poly-L-lysine and poly-L-glutamic acid. Journal of the American Chemical Society, 127 (21). 7712 - 7720. ISSN 0002-7863

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Abstract

UV resonance Raman (UVR) spectroscopy was used to examine the solution conformation of poly-L-lysine (PLL) and poly-L-glutamic acid (PGA) in their non-α-helical states. UVR measurements indicate that PLL (at pH = 2) and PGA (at pH = 9) exist mainly in a mixture of polyproline II (PPII) and a novel left-handed 2.51-helical conformation, which is an extended β-strand-like conformation with Ψ ≈ 1170° and Φ ≈ 130°. Both of these conformations are highly exposed to water. The energies of these conformations are very similar. We see no evidence of any disordered "random coil" states. In addition, we find that a PLL and PGA mixture at neutral pH is ∼60% β-sheet and contains PPII and extended 2.5 1-helix conformations. The β-sheet conformation shows little evidence of amide backbone hydrogen bonding to water. We also developed a method to estimate the distribution of Ψ Ramachandran angles for these conformations, which we used to estimate a Ψ Ramachandran angle energy landscape. We believe that these are the first experimental studies to give direct information on protein and peptide energy landscapes. © 2005 American Chemical Society.


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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Mikhonin, AV
Myshakina, NS
Bykov, SV
Asher, SAasher@pitt.eduASHER
Date: 1 June 2005
Date Type: Publication
Journal or Publication Title: Journal of the American Chemical Society
Volume: 127
Number: 21
Page Range: 7712 - 7720
DOI or Unique Handle: 10.1021/ja044636s
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 0002-7863
MeSH Headings: Circular Dichroism; Models, Molecular; Peptides--chemistry; Polyglutamic Acid--chemistry; Polylysine--chemistry; Protein Conformation; Protein Folding; Protein Structure, Secondary; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Thermodynamics
PubMed ID: 15913361
Date Deposited: 08 Feb 2013 21:14
Last Modified: 02 Feb 2019 15:59
URI: http://d-scholarship.pitt.edu/id/eprint/17209

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