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.
| Original language | English |
|---|---|
| Pages (from-to) | 444-447 |
| Number of pages | 4 |
| Journal | Physical Chemistry Chemical Physics |
| Volume | 15 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Jan 14 2013 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Physics and Astronomy(all)
- Physical and Theoretical Chemistry
Cite this
Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide inhibitor siamycin I revealed through synchrotron radiation circular dichroism. / Phillips-Jones, Mary K.; Patching, Simon G.; Edara, Shalini; Nakayama, Jiro; Hussain, Rohanah; Siligardi, Giuliano.
In: Physical Chemistry Chemical Physics, Vol. 15, No. 2, 14.01.2013, p. 444-447.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide inhibitor siamycin I revealed through synchrotron radiation circular dichroism
AU - Phillips-Jones, Mary K.
AU - Patching, Simon G.
AU - Edara, Shalini
AU - Nakayama, Jiro
AU - Hussain, Rohanah
AU - Siligardi, Giuliano
PY - 2013/1/14
Y1 - 2013/1/14
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84870895754&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84870895754&partnerID=8YFLogxK
U2 - 10.1039/c2cp43722h
DO - 10.1039/c2cp43722h
M3 - Article
C2 - 23183669
AN - SCOPUS:84870895754
VL - 15
SP - 444
EP - 447
JO - Physical Chemistry Chemical Physics
JF - Physical Chemistry Chemical Physics
SN - 1463-9076
IS - 2
ER -