Extensive counter-ion interactions seen at the surface of subtilisin in an aqueous medium-Reference-Cited by-同舟云学术

Extensive counter-ion interactions seen at the surface of subtilisin in an aqueous medium

Published:2014 Issue:69 Volume:4 Page:36771-36776
ISSN:2046-2069
Container-title:RSC Adv.
language:en
Short-container-title:RSC Adv.

Author:

Cianci Michele¹²^ORCID,Negroni Jacopo¹²,Helliwell John R.³⁴⁵,Halling Peter J.⁶⁷⁸⁹

Affiliation:

1. European Molecular Biology Laboratory c/o DESY

2. 22603 Hamburg, Germany

3. School of Chemistry

4. University of Manchester

5. Manchester, UK

6. WestCHEM

7. Department of P & A Chemistry

8. University of Strathclyde

9. Glasgow G1 1XL, UK

Abstract

The extent of counter-ion interaction within subtilisin in aqueous medium has been investigated using CsCl soak and anomalous diffraction, revealing that in aqueous salt solutions ions can bind at defined points around the protein surface.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2014/RA/C4RA06448H

Reference25 articles.

1. How Hofmeister ion interactions affect protein stability

2. Getting Specific About Specific Ion Effects

3. Competition among Metal Ions for Protein Binding Sites: Determinants of Metal Ion Selectivity in Proteins

4. Ions at Aqueous Interfaces: From Water Surface to Hydrated Proteins

5. Specific ion effects in colloidal and biological systems

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