Protein States and Proteinquakes

After photodissociation of carbon monoxide bound to myoglobin, the protein relaxes to the deoxy equilibrium structure in a quake-like motion. Investigation of the proteinquake and of related intramolecular equilibrium motions shows that states and motions have a hierarchical glasslike structure.

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1985-08, Vol.82 (15), p.5000-5004
Main Authors: Ansari, Anjum, Berendzen, Joel, Bowne, Samuel F., Frauenfelder, Hans, Icko E. T. Iben, Sauke, Todd B., Shyamsunder, Erramilli, Young, Robert D.
Format: Article
Language:English
Subjects:
Activation energy
Biological and medical sciences
Biophysical Phenomena
Biophysics
Carbon Monoxide - metabolism
Coordinate systems
Fundamental and applied biological sciences. Psychology
Gibbs free energy
Lead
Ligands
Molecular biophysics
Motion
Myoglobin - metabolism
Photolysis
Protein Conformation
Raman scattering
Spectrum Analysis, Raman
Structure in molecular biology
Temperature dependence
Thermodynamic equilibrium
Thermodynamics
Tridimensional structure
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Description
Summary:After photodissociation of carbon monoxide bound to myoglobin, the protein relaxes to the deoxy equilibrium structure in a quake-like motion. Investigation of the proteinquake and of related intramolecular equilibrium motions shows that states and motions have a hierarchical glasslike structure.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.82.15.5000