Issue 84, 2013
From the journal:

Chemical Communications

Detection of salt bridges to lysines in solution in barnase†

Mike P. Williamson,*a   Andrea M. Hounslow,a   Joe Ford,a   Kyle Fowler,a   Max Hebditcha  and  Poul Erik Hansenb  

* Corresponding authors

a Dept of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK
E-mail: m.williamson@sheffield.ac.uk
Fax: +44 (0)114 2224243
Tel: +44 (0)114 2224224

b Dept of Science, Systems and Models, 18.1, Roskilde University, Universitetsvej 1, PO Box 260, DK-4000 Roskilde, Denmark
E-mail: poulerik@ruc.dk
Fax: +45 46743011
Tel: +45 46742432

Abstract

We show that salt bridges involving lysines can be detected by deuterium isotope effects on NMR chemical shifts of the sidechain amine. Lys27 in the ribonuclease barnase is salt bridged, and mutation of Arg69 to Lys retains a partially buried salt bridge. The salt bridges are functionally important.

Graphical abstract: Detection of salt bridges to lysines in solution in barnase

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Article information

DOI
https://doi.org/10.1039/C3CC45602A
Article type
Communication
Submitted
23 Jul 2013
Accepted
05 Sep 2013
First published
05 Sep 2013

Chem. Commun., 2013,49, 9824-9826

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Detection of salt bridges to lysines in solution in barnase

M. P. Williamson, A. M. Hounslow, J. Ford, K. Fowler, M. Hebditch and P. E. Hansen, Chem. Commun., 2013, 49, 9824 DOI: 10.1039/C3CC45602A

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