Dissecting Electrostatic Contributions to Folding and Self-Assembly Using Designed Multicomponent Peptide Systems-Reference-Cited by-同舟云学术

Dissecting Electrostatic Contributions to Folding and Self-Assembly Using Designed Multicomponent Peptide Systems

Published:2016-03-24 Issue:13 Volume:138 Page:4362-4367
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Parmar Avanish S.¹,James Jose K.²,Grisham Daniel R.²,Pike Douglas H.²,Nanda Vikas²

Affiliation:

1. Department of Physics, Indian Institute of Technology (Banaras Hindu University), Varanasi 221005, Uttar Pradesh, India

2. Center for Advanced Biotechnology and Medicine, Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers University, 679 Hoes Lane West, Piscataway, New Jersey 08854, United States

Funder

NIH Office of the Director

Science and Engineering Research Board

National Institute of General Medical Sciences

Division of Materials Research

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.5b10304

Reference71 articles.

1. Prediction of Collagen Stability from Amino Acid Sequence

2. Electrostatic Interactions Involving Lysine Make Major Contributions to Collagen Triple-Helix Stability

3. Peptide investigations of pairwise interactions in the collagen triple-helix

4. Gly-X-Y Tripeptide Frequencies in Collagen: A Context for Host–Guest Triple-Helical Peptides

5. Positional Preferences of Ionizable Residues in Gly-X-YTriplets of the Collagen Triple-helix

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