A hierarchy of functionally important relaxations within myoglobin based on solvent effects, mutations and kinetic model

Author:

Dantsker David,Samuni Uri,Friedman Joel M.,Agmon Noam

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference79 articles.

1. The energy landscapes and motions of proteins;Frauenfelder;Science,1991

2. The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin;Frauenfelder;Proc. Natl. Acad. Sci. U. S. A.,2001

3. Hemoglobin and Myoglobin in their Reactions with Ligands;Antonini,1971

4. Dynamics of ligand binding to myoglobin;Austin;Biochemistry,1975

5. Solvent viscosity and protein dynamics;Beece;Biochemistry,1980

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