Dynamic allostery of protein alpha helical coiled-coils

Dynamic allostery of protein alpha helical coiled-coils

consistent with experimental results. A further prediction is a quantitative increase in the effective stiffness of the coiled-coil without any change in inherent flexibility of the individual helices. The model provides a possible and experimentally testable mechanism for transmission of informatio...

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Veröffentlicht in:Journal of the Royal Society interface 2006-02, Vol.3 (6), p.125-138
Hauptverfasser: Hawkins, Rhoda J, McLeish, Tom C.B
Format: Artikel
Sprache:eng
Schlagworte:
Allostery
Binding Sites
Biophysics
Coiled-Coil
Computer Simulation
Dyneins - chemistry
Dyneins - ultrastructure
Energy Transfer
Isomerism
Kinetics
Microtubules - chemistry
Microtubules - ultrastructure
Models, Chemical
Models, Molecular
Molecular Motor Proteins - chemistry
Motion
Physics
Protein Binding
Protein Conformation
Protein Dynamics
Protein Structure, Secondary
Theory
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Beschreibung
Zusammenfassung:consistent with experimental results. A further prediction is a quantitative increase in the effective stiffness of the coiled-coil without any change in inherent flexibility of the individual helices. The model provides a possible and experimentally testable mechanism for transmission of information through the alpha helical coiled-coil of dynein.
ISSN:1742-5689
1742-5662
DOI:10.1098/rsif.2005.0068