Journal Article

PreJuSER-541

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Direct Observation of Correlated Interdomain Motion in Alcohol Dehydrogenase

Biehl, R.FZJ* ; Hoffmann, B.FZJ* ; Monkenbusch, M.FZJ* ; Falus, P. ; Préost, S. ; Merkel, R.FZJ* ; Richter, D.FZJ*

2008
APS College Park, Md.

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Please use a persistent id in citations: http://hdl.handle.net/2128/7176  doi:10.1103/PhysRevLett.101.138102

Abstract: Interdomain motions in proteins are essential to enable or promote biochemical function. Neutron spinecho spectroscopy is used to directly observe the domain dynamics of the protein alcohol dehydrogenase. The collective motion of domains as revealed by their coherent form factor relates to the cleft opening dynamics between the binding and the catalytic domains enabling binding and release of the functional important cofactor. The cleft opening mode hardens as a result of an overall stiffening of the domain complex due to the binding of the cofactor.

Keyword(s): J

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. Biomechanik (IBN-4)
2. Neutronenstreuung (IFF-5)
3. Streumethoden (IFF-4)
4. JCNS (Jülich Centre for Neutron Science JCNS (JCNS) ; JCNS)

Research Program(s):

1. Kondensierte Materie (P54)
2. Großgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI) (P55)

Appears in the scientific report 2008

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Database coverage:
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