Opposing roles of organic salts on mini-protein structure-Reference-Cited by-同舟云学术

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Opposing roles of organic salts on mini-protein structure

Published:2024 Issue:11 Volume:26 Page:8973-8981
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Lee Pei-Yin¹,Singh Onkar²,Nanajkar Neha³,Bermudez Harry²^ORCID,Matysiak Silvina⁴^ORCID

Affiliation:

1. Chemical Physics Program, Institute for Physical Science and Technology, University of Maryland, College Park, USA

2. Department of Polymer Science and Engineering, University of Massachusetts, Amherst, MA, USA

3. Department of Biology, University of Maryland, College Park, USA

4. Fischell Department of Bioengineering, University of Maryland, College Park, USA

Abstract

Exploring impact of [EMIM][Cl] and [Chol][Cl] on Trp-cage and Trpzip4 mini-proteins' environments and structures using computational and experimental methods.

Funder

Division of Chemical, Bioengineering, Environmental, and Transport Systems

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/CP/D3CP05607D

Reference66 articles.

1. How ionic liquids can help to stabilize native proteins

2. Protein stabilization and enzyme activation in ionic liquids: specific ion effects

3. Use of Ionic Liquids in Protein and DNA Chemistry

4. How ion properties determine the stability of a lipase enzyme in ionic liquids: A molecular dynamics study

5. Protein Denaturation by Ionic Liquids and the Hofmeister Series: A Case Study of Aqueous Solutions of Ribonuclease A

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