The Effects of Chain Length and Thermal Denaturation on Helix-Forming Peptides: A Mode-Specific Analysis Using 2D FT-IR-Reference-Cited by-同舟云学术

The Effects of Chain Length and Thermal Denaturation on Helix-Forming Peptides: A Mode-Specific Analysis Using 2D FT-IR

Published:1997-11-01 Issue:46 Volume:119 Page:11282-11294
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Graff D. K.¹,Pastrana-Rios B.¹,Venyaminov S. Yu.¹,Prendergast F. G.¹

Affiliation:

1. Contribution from the Department of Pharmacology, The Mayo Clinic and Foundation, 1417 Guggenheim, 200 First Street SW, Rochester, Minnesota 55905, and University of Puerto Rico, Mayaguez Campus, Office M224, Post Street, Mayaguez, Puerto Rico 00681-5000

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja970512m

Reference60 articles.

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

2. Measuring the Strength of Side-Chain Hydrogen Bonds in Peptide Helixes: The Gln.cntdot.Asp (i, i + 4) Interaction

3. Modulation of the helical stability of a model peptide by ionic residues

4. Effect of amino acid ion pairs on peptide helicity

5. Incorporation of pairwise interactions into the Lifson-Roig model for helix prediction

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