Protein Dynamics in an Intermediate State of Myoglobin: Optical Absorption, Resonance Raman Spectroscopy, and X-Ray Structure Analysis
Open Access
- 30 April 2000
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 78 (4) , 2081-2092
- https://doi.org/10.1016/s0006-3495(00)76755-5
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- Spectroscopic Evidence for Nanosecond Protein Relaxation after Photodissociation of Myoglobin−COBiochemistry, 1998
- Photodissociation and Rebinding of H2O to Ferrous Sperm Whale MyoglobinJournal of the American Chemical Society, 1998
- Photolysis of the Carbon Monoxide Complex of Myoglobin: Nanosecond Time-Resolved CrystallographyScience, 1996
- Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemesBiospectroscopy, 1996
- Conformational Properties of Nickel(II) Octaethylporphyrin in Solution. 2. A Low-Temperature Optical Absorption Spectroscopy StudyThe Journal of Physical Chemistry, 1996
- Relaxation of non-equilibrium states of myoglobin studied by Mössbauer spectroscopyHyperfine Interactions, 1994
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Model bias in macromolecular crystal structuresActa Crystallographica Section A Foundations of Crystallography, 1992
- Investigations of optical line shapes and kinetic hole burning in myoglobinBiochemistry, 1991
- Spectral Broadening in BiomoleculesPhysical Review Letters, 1986