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Issue 2, 2013
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Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptideinhibitor siamycin I revealed through synchrotron radiation circular dichroism

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Abstract

The suitability of synchrotron radiation circular dichroism spectroscopy (SRCD) for studying interactions between the tricyclic peptide inhibitor siamycin I and the intact FsrC membrane sensor kinase in detergent micelles has been established. In the present study, tertiary structural changes demonstrate that inhibitor binding occurs at a different, non-overlapping site to the native ligand, GBAP.

Graphical abstract: Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide inhibitor siamycin I revealed through synchrotron radiation circular dichroism

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Article information


Submitted
22 Oct 2012
Accepted
13 Nov 2012
First published
14 Nov 2012

Phys. Chem. Chem. Phys., 2013,15, 444-447
Article type
Communication

Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide inhibitor siamycin I revealed through synchrotron radiation circular dichroism

M. K. Phillips-Jones, S. G. Patching, S. Edara, J. Nakayama, R. Hussain and G. Siligardi, Phys. Chem. Chem. Phys., 2013, 15, 444
DOI: 10.1039/C2CP43722H

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