Identifying Residual Structure in Intrinsically Disordered Systems: A 2D IR Spectroscopic Study of the GVGXPGVG Peptide-Reference-Cited by-同舟云学术

Identifying Residual Structure in Intrinsically Disordered Systems: A 2D IR Spectroscopic Study of the GVGXPGVG Peptide

Published:2012-03-07 Issue:11 Volume:134 Page:5032-5035
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Lessing Joshua¹,Roy Santanu²,Reppert Mike¹,Baer Marcel³,Marx Dominik³,Jansen Thomas La Cour²,Knoester Jasper²,Tokmakoff Andrei¹

Affiliation:

1. Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States

2. Center for Theoretical Physics and Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands

3. Lehrstuhl für Theoretische Chemie, Ruhr-Universität Bochum, 44780 Bochum, Germany

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja2114135

Reference33 articles.

1. Defining Solution Conformations of Small Linear Peptides

2. NMR evidence of a short linear peptide that folds into a .beta.-hairpin in aqueous solution

3. A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin

4. Interstrand Side Chain−Side Chain Interactions in a Designed β-Hairpin: Significance of Both Lateral and Diagonal Pairings

5. Analysis of the factors that stabilize a designed two-stranded antiparallel β-sheet

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