Article (Scientific journals)
An alternative flexible conformation of the E. coli HUbeta(2) protein: structural, dynamics, and functional aspects.
Garnier, N.; Loth, K.; Coste, F. et al.
2011In European Biophysics Journal, 40 (2), p. 117-129
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Abstract :
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Garnier, N.
Loth, K.
Coste, F.
Augustyniak, R.
Nadan, V.
Damblon, Christian ;  Université de Liège - ULiège > Département de chimie (sciences) > Chimie biologique structurale
Castaing, B.
Language :
English
Title :
An alternative flexible conformation of the E. coli HUbeta(2) protein: structural, dynamics, and functional aspects.
Publication date :
2011
Journal title :
European Biophysics Journal
ISSN :
0175-7571
eISSN :
1432-1017
Publisher :
Springer Verlag, Berlin, Germany
Volume :
40
Issue :
2
Pages :
117-129
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 19 January 2011

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