Reference : An alternative flexible conformation of the E. coli HUbeta(2) protein: structural, dynam...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/82451
An alternative flexible conformation of the E. coli HUbeta(2) protein: structural, dynamics, and functional aspects.
English
Garnier, N. [> > > >]
Loth, K. [> > > >]
Coste, F. [> > > >]
Augustyniak, R. [> > > >]
Nadan, V. [> > > >]
Damblon, Christian mailto [Université de Liège - ULg > Département de chimie (sciences) > Chimie biologique structurale >]
Castaing, B. [> > > >]
2011
European Biophysics Journal [=EBJ]
Springer Verlag
40
2
117-129
Yes (verified by ORBi)
International
0175-7571
Berlin
Germany
[en] The histone-like HU protein is the major nucleoid-associated protein involved in the dynamics and structure of the bacterial chromosome. Under physiological conditions, the three possible dimeric forms of the E. coli HU protein (EcHUalpha(2), EcHUbeta(2), and EcHUalphabeta) are in thermal equilibrium between two dimeric conformations (N(2) <--> I(2)) varying in their secondary structure content. High-temperature molecular dynamics simulations combined with NMR experiments provide information about structural and dynamics features at the atomic level for the N(2) to I(2) thermal transition of the EcHUbeta(2) homodimer. On the basis of these data, a realistic 3D model is proposed for the major I(2) conformation of EcHUbeta(2). This model is in agreement with previous experimental data.
http://hdl.handle.net/2268/82451
10.1007/s00249-010-0630-y

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