The Anomalous Infrared Amide I Intensity Distribution in 13C Isotopically Labeled Peptide β-Sheets Comes from Extended, Multiple-Stranded Structures. An ab Initio Study-Reference-Cited by-同舟云学术

The Anomalous Infrared Amide I Intensity Distribution in 13C Isotopically Labeled Peptide β-Sheets Comes from Extended, Multiple-Stranded Structures. An ab Initio Study

Published:2001-05-31 Issue:25 Volume:123 Page:6142-6150
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Kubelka Jan¹,Keiderling Timothy A.¹

Affiliation:

1. Contribution from the Department of Chemistry (M/C 111), University of Illinois at Chicago, 845 West Taylor Street, Room 4500 SES, Chicago, Illinois 60607-7061

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja010270x

Reference36 articles.

1. The Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure

2. Use of a Designed Triple-Stranded Antiparallel β-Sheet To Probe β-Sheet Cooperativity in Aqueous Solution

3. Minimal model systems for β-sheet secondary structure in proteins

4. Cooperative Interaction between the Three Strands of a Designed Antiparallel β-Sheet

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