Spin relaxation enhancement confirms dominance of extended conformations in short alanine peptides

Kang Chen, Zhigang Liu, Chunhui Zhou, W. Clay Bracken, Neville R. Kallenbach

Research output: Contribution to journalArticle

Abstract

(Figure Presented) Local order goes with random coil: An ensemble of peptide structures is generated with over 90% extended conformation for Ala and Pro. The population-averaged long-range distance from the N-terminal spin-label residue (see picture, red dot) to the C-terminal amide proton of Ala (blue dots) is fully consistent with the results from NMR spin relaxation measurements.

Original languageEnglish (US)
Pages (from-to)9036-9039
Number of pages4
JournalAngewandte Chemie - International Edition
Volume46
Issue number47
DOIs
StatePublished - 2007

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Spin Labels
Amides
Alanine
Conformations
Protons
Nuclear magnetic resonance
Peptides

Keywords

  • Intramolecular distances
  • NMR spectroscopy
  • Peptides
  • Protein folding

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Spin relaxation enhancement confirms dominance of extended conformations in short alanine peptides. / Chen, Kang; Liu, Zhigang; Zhou, Chunhui; Bracken, W. Clay; Kallenbach, Neville R.

In: Angewandte Chemie - International Edition, Vol. 46, No. 47, 2007, p. 9036-9039.

Research output: Contribution to journalArticle

Chen, Kang ; Liu, Zhigang ; Zhou, Chunhui ; Bracken, W. Clay ; Kallenbach, Neville R. / Spin relaxation enhancement confirms dominance of extended conformations in short alanine peptides. In: Angewandte Chemie - International Edition. 2007 ; Vol. 46, No. 47. pp. 9036-9039.
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