Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities-Reference-Cited by-同舟云学术

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Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities

Published:2017-07-19 Issue:8 Volume:50 Page:1875-1882
ISSN:0001-4842
Container-title:Accounts of Chemical Research
language:en
Short-container-title:Acc. Chem. Res.

Author:

Ardejani Maziar S.¹,Powers Evan T.¹,Kelly Jeffery W.¹²³^ORCID

Affiliation:

1. Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States

2. Department of Molecular Medicine, The Scripps Research Institute, La Jolla, California 92037, United States

3. The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

General Medicine,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.accounts.7b00195

Reference59 articles.

1. Some Factors in the Interpretation of Protein Denaturation

2. Contribution of Hydrophobic Interactions to the Stability of the Globular Conformation of Proteins

3. Affinities of amino acid side chains for solvent water

4. Hydrophobicity of Amino Acid Residues in Globular Proteins

5. Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area

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