Long-Range Interactions Dominate the Inverse-Temperature Dependence of Polypeptide Hydration Free Energies

Direct, all-atom calculations of the free energy of hydration of aqueous deca-alanine structures --- holistically including backbone and side-chain interactions together --- show that attractive interactions and the thermal expansion of the solvent explain the inverse temperature signatures that hav...

Full description

Saved in:
Bibliographic Details
Published in:arXiv.org 2019-01
Main Authors: Tomar, Dheeraj S, Paulaitis, Michael E, Pratt, Lawrence R, Asthagiri, D
Format: Article
Language:English
Subjects:
Alanine
Free energy
Hydration
Proteins
Temperature dependence
Thermal expansion
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Direct, all-atom calculations of the free energy of hydration of aqueous deca-alanine structures --- holistically including backbone and side-chain interactions together --- show that attractive interactions and the thermal expansion of the solvent explain the inverse temperature signatures that have been interpreted traditionally in favor of hydrophobic mechanisms for stabilizing the structure and function of soluble proteins.
ISSN:2331-8422