Reference : Downhill Binding Energy Surface of the Barnase-Barstar Complex
Scientific journals : Other
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/3769
Downhill Binding Energy Surface of the Barnase-Barstar Complex
English
Wang, Ling [> >]
Siu, Shirley W. I. [> >]
Gu, Wei mailto []
Helms, Volkhard [> >]
2010
Biopolymers
Wiley Interscience
93
11
977-985
Yes (verified by ORBilu)
International
0006-3525
1097-0282
New York
NY
[en] We have employed biased molecular dynamics simulations in explicit solvent to characterize the one-dimensional potential of mean force for the dissociation process of the barnase-barstar protein-protein complex. Unbinding of barstar from wild-type barnase was compared with dissociation from four charge-deletion mutants of barnase. Interestingly, we find in all cases that unbinding of barnase and barstar is an uphill process on a smooth, tilted energy landscape. The total free energy difference between the dissociated and bound state was similar for wild-type barnase-barstar and for the R87A mutant of barnase. The values for the three other mutant barnase mutants K27A, R59A, and R83Q were only about half as much. Besides, we have analyzed the conformational dynamics of important residues at the barnase-barstar interface. In the bound state, their conformational fluctuations are reduced relatively to the free state because of the formation of intermolecular contacts. Interestingly, we find that some residues also show decreased mobility at intermediate stages of the unbinding process suggesting that these residues may be involved in the first contacts being formed on binding. (C) 2010 Wiley Periodicals, Inc. Biopolymers 93: 977-985, 2010.
http://hdl.handle.net/10993/3769
10.1002/bip.21507

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