Hydrophilic Interactions Dominate the Inverse Temperature Dependence of Polypeptide Hydration Free Energies Attributed to Hydrophobicity-Reference-Cited by-同舟云学术

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Hydrophilic Interactions Dominate the Inverse Temperature Dependence of Polypeptide Hydration Free Energies Attributed to Hydrophobicity

Published:2020-11-10 Issue:22 Volume:11 Page:9965-9970
ISSN:1948-7185
Container-title:The Journal of Physical Chemistry Letters
language:en
Short-container-title:J. Phys. Chem. Lett.

Author:

Tomar Dheeraj S.¹,Paulaitis Michael E.²^ORCID,Pratt Lawrence R.³^ORCID,Asthagiri Dilipkumar N.⁴^ORCID

Affiliation:

1. Xilio Therapeutics Inc., Waltham, Massachusetts 02451, United States

2. Center for Nanomedicine, Johns Hopkins School of Medicine, Baltimore, Maryland 21231, United States

3. Department of Chemical and Biomolecular Engineering, Tulane University, New Orleans, Louisiana 70118, United States

4. Department of Chemical and Biomolecular Engineering, Rice University, Houston, Texas 77005, United States

Publisher

American Chemical Society (ACS)

Subject

General Materials Science,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpclett.0c02972

Reference41 articles.

1. Principles that Govern the Folding of Protein Chains

2. Some Factors in the Interpretation of Protein Denaturation

3. Dominant forces in protein folding

4. The Protein Folding Problem

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

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