Protein states and proteinquakes.
- 1 August 1985
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 82 (15) , 5000-5004
- https://doi.org/10.1073/pnas.82.15.5000
Abstract
After photodissociation of CO 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.Keywords
This publication has 26 references indexed in Scilit:
- Structural domains in proteins and their role in the dynamics of protein functionProgress in Biophysics and Molecular Biology, 1983
- Hemoglobin tertiary structural change on ligand binding its role in the co-operative mechanismJournal of Molecular Biology, 1983
- Relaxation processes on a picosecond time scale in hemoglobin and poly(L‐alanine) observed by millimeter‐wave spectroscopyBiopolymers, 1983
- A comparison of the heme electronic states in equilibrium and nonequilibrium protein conformations of high-spin ferrous hemoproteins low temperature magnetic circular dichroism studiesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Dynamics of metmyoglobin crystals investigated by nuclear gamma resonance absorptionJournal of Molecular Biology, 1981
- Structure and refinement of oxymyoglobin at 1·6 Å resolutionJournal of Molecular Biology, 1980
- Temperature-dependent X-ray diffraction as a probe of protein structural dynamicsNature, 1979
- The physical aspects of energy transduction in biological systemsQuarterly Reviews of Biophysics, 1978
- Low temperature photodissociation studies of ferrous hemoglobin and myoglobin complexes by Mössbauer spectroscopyBiochimica et Biophysica Acta (BBA) - General Subjects, 1976
- Dynamics of ligand binding to myoglobinBiochemistry, 1975