Unravelling the hydrophobicity of urea in water using thermodiffusion: implications for protein denaturation-Reference-Cited by-同舟云学术

Unravelling the hydrophobicity of urea in water using thermodiffusion: implications for protein denaturation

Published:2018 Issue:2 Volume:20 Page:1012-1020
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Niether Doreen¹²³⁴^ORCID,Di Lecce Silvia⁵⁶⁷⁸^ORCID,Bresme Fernando⁵⁶⁷⁸⁵^ORCID,Wiegand Simone¹²³⁴⁹

Affiliation:

1. ICS-3 Soft Condensed Matter

2. Forschungszentrum Jülich GmbH

3. D-52428 Jülich

4. Germany

5. Department of Chemistry

6. Imperial College

7. London SW7 2AZ

8. UK

9. Department für Chemie-Physikalische Chemie

Abstract

Sensitivity of thermodiffusion to urea–water interactions was studied experimentally and by NEMD simulations, identifying the hydrophobic behaviour of urea.

Funder

Engineering and Physical Sciences Research Council

Horizon 2020

Norges Forskningsråd

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CP/C7CP05843H

Reference54 articles.

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4. The hydrogen bond network structure within the hydration shell around simple osmolytes: Urea, tetramethylurea, and trimethylamine-N-oxide, investigated using both a fixed charge and a polarizable water model

5. Computer simulations on aqueous solutions of some non-electrolytes

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