Biopolymer Conformational Distributions from Solid-State NMR: α-Helix and 310-Helix Contents of a Helical Peptide-Reference-Cited by-同舟云学术

Biopolymer Conformational Distributions from Solid-State NMR: α-Helix and 310-Helix Contents of a Helical Peptide

Published:1998-07-01 Issue:28 Volume:120 Page:7039-7048
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Long Henry W.¹,Tycko Robert¹

Affiliation:

1. Contribution from the Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja974277j

Reference49 articles.

1. Kallenbach, N. R.; Lyu, P.; Zhou, H. InCircular Dichroism and theConformational Analysis of Biomolecules; Fasman, G. D., Ed.; Plenum Press: New York, 1996; pp 201−259.

2. Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design.

3. Unusually stable helix formation in short alanine-based peptides.

4. Relative helix-forming tendencies of nonpolar amino acids

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