Design of Short Linear Peptides That Show Hydrogen Bonding Constraints in Water-Reference-Cited by-同舟云学术

Design of Short Linear Peptides That Show Hydrogen Bonding Constraints in Water

Published:2010-03-17 Issue:13 Volume:132 Page:4508-4509
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Song Benben¹,Kibler Patrick¹,Malde Alpeshkumar¹,Kodukula Krishna¹,Galande Amit K.¹

Affiliation:

1. Center for Advanced Drug Research (CADRE), SRI International, Harrisonburg, Virginia 22802, and School of Chemistry and Molecular Biosciences (SCMB), The University of Queensland, St. Lucia QLD 4072, Australia

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja905341p

Reference13 articles.

1. Perczel, A. and Hollosi, M.InCircular Dichroism and the Conformational Analysis of Biomolecules;Fasman, G. D., Eds.Plenum Publishing Corporation:New York, 1996; Vol. 28, pp5−380.

2. A conformational study of peptides with the general structure Ac-L-Xaa-Pro-D-Xaa-L-Xaa-NH2: spectroscopic evidence for a peptide with significant .beta.-turn character in water and in dimethyl sulfoxide

3. Structural characteristics of .alpha.-helical peptide molecules containing Aib residues

4. Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an α-helical region of carboxypeptidase A

5. Hydrogen-bonding classes in proteins and their contribution to the unfolding reaction

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