Quantitative evaluation of contributions to electron paramagnetic resonance line widths in ferric hemoglobin single crystals
- 1 February 1979
- journal article
- research article
- Published by Elsevier in Biophysical Journal
- Vol. 25 (2), 313-322
- https://doi.org/10.1016/s0006-3495(79)85294-7
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Crystalline state disorder and hyperfine component line widths in ferric hemoglobin chainsBiophysical Journal, 1979
- The structure of horse methaemoglobin at 2.0 Å resolutionJournal of Molecular Biology, 1977
- 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
- MEASUREMENT OF STRUCTURAL AND FREE ENERGY CHANGES IN HEMOGLOBIN BY HYDROGEN EXCHANGE METHODSAnnals of the New York Academy of Sciences, 1975
- ELECTRON NUCLEAR DOUBLE RESONANCE (ENDOR) INVESTIGATION ON MYOGLOBIN AND HEMOGLOBIN *Annals of the New York Academy of Sciences, 1973
- Electron nuclear double resonance studies on heme proteins: Determination of the interaction of Fe3+ with its ligand nitrogens in metmyoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1972
- A Neutron Diffraction Analysis of Myoglobin. III. Hydrogen-Deuterium Bonding in Side ChainsCold Spring Harbor Symposia on Quantitative Biology, 1972
- Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic ModelNature, 1968
- Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution : (I) X-ray AnalysisNature, 1968