Probing the Internal Dynamics and Shape of Simple Peptides in Urea, Guanidinium Hydrochloride, and Proline Solutions with Time-Resolved Fluorescence Anisotropy and Atomistic Cosolvent Simulations-Reference-Cited by-同舟云学术

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Probing the Internal Dynamics and Shape of Simple Peptides in Urea, Guanidinium Hydrochloride, and Proline Solutions with Time-Resolved Fluorescence Anisotropy and Atomistic Cosolvent Simulations

Published:2021-09-24 Issue:39 Volume:125 Page:10972-10984
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Jas Gouri S.¹^ORCID,Childs Ed W.²,Middaugh C. Russell¹,Kuczera Krzysztof³^ORCID

Affiliation:

1. Department of Pharmaceutical Chemistry, The University of Kansas, Lawrence, Kansas 66047, United States

2. Department of Surgery, Morehouse School of Medicine, Atlanta, Georgia 30310, United States

3. Department of Chemistry and Department of Molecular Biosciences, The University of Kansas, Lawrence, Kansas 66045, United States

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.1c06838

Reference51 articles.

1. THE ORIGINS OF LIFE

2. Cell potassium and the significance of osmolarity in vertebrates

3. Solute compatibility with enzyme function and structure: Rationales for the selection of osmotic agents and end-products of anaerobic metabolism in marine invertebrates

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