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UV resonance Raman elucidation of the terminal and internal peptide bond conformations of crystalline and solution oligoglycines

Bykov, SV and Asher, SA (2010) UV resonance Raman elucidation of the terminal and internal peptide bond conformations of crystalline and solution oligoglycines. Journal of Physical Chemistry Letters, 1 (1). 269 - 271.

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Spectroscopic investigations of macromolecules generally attempt to interpret the measured spectra in terms of the summed contributions of the different molecular fragments. This is the basis of the local-mode approximation in vibrational spectroscopy. In the case of resonance Raman spectroscopy, independent contributions of molecular fragments require both a local-mode-like behavior and the uncoupled electronic transitions. Here, we show that the deep-UV resonance Raman spectra of aqueous solution-phase oligoglycines show independent peptide bond molecular fragment contributions, indicating that peptide bond electronic transitions and vibrational modes are uncoupled. We utilize this result to separately determine the conformational distributions of the internal and penultimate peptide bonds of oligoglycines. Our data indicate that in aqueous solution, the oligoglycine terminal residues populate conformations similar to those found in crystals (31-helices and β-strands) but with a broader distribution, while the internal peptide bond conformations are centered around the 31-helix Ramachandran angles. © 2009 American Chemical Society.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Bykov, SV
Asher, SAasher@pitt.eduASHER
Date: 1 January 2010
Date Type: Publication
Journal or Publication Title: Journal of Physical Chemistry Letters
Volume: 1
Number: 1
Page Range: 269 - 271
DOI or Unique Handle: 10.1021/jz900117u
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
PubMed Central ID: PMC2908416
PubMed ID: 20657703
Date Deposited: 08 Feb 2013 21:04
Last Modified: 22 Jun 2021 12:56


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