High-Field 1H MAS and 15N CP-MAS NMR Studies of Alanine Tripeptides and Oligomers: Distinction of Antiparallel and Parallel β-Sheet Structures and Two Crystallographically Independent Molecules-Reference-Cited by-同舟云学术

High-Field 1H MAS and 15N CP-MAS NMR Studies of Alanine Tripeptides and Oligomers: Distinction of Antiparallel and Parallel β-Sheet Structures and Two Crystallographically Independent Molecules

Published:2007-07-11 Issue:30 Volume:111 Page:9172-9178
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Suzuki Yu¹,Okonogi Michi¹,Yamauchi Kazuo¹,Kurosu Hiromichi¹,Tansho Masataka¹,Shimizu Tadashi¹,Saitô Hazime¹,Asakura Tetsuo¹

Affiliation:

1. Department of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16, Nakacho, Koganei, Tokyo 184-8588, Japan, Graduate School of Humanities and Sciences, Nara Women's University, Kitauoya-Nishimachi, Nara 630-8506, Japan, and National Institute for Material Science, 3-13 Sakura, Tsukuba, Ibaraki 305-0003, Japan

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp072755z

Reference47 articles.

1. Configurations of Polypeptide Chains With Favored Orientations Around Single Bonds: Two New Pleated Sheets

2. The structure of the tripeptide L-alanyl-L-alanyl-L-alanine

3. L-Alanyl-L-alanyl-L-alanine: Parallel pleated sheet arrangement in unhydrated crystal structure, and comparisons with the antiparallel sheet structure

4. Structural Analysis of Alanine Tripeptide with Antiparallel and Parallel β-Sheet Structures in Relation to the Analysis of Mixed β-Sheet Structures in Samia cynthia ricini Silk Protein Fiber Using Solid-State NMR Spectroscopy

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