The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Conformational substates in a protein: structure and dynamics of metmyoglobin at 80 K.
Open accessAbstract
The crystal structure of sperm whale metmyoglobin has been determined at 80 K to a resolution of 2A. The overall structure at 80 K is similar to that at 300 K except that the volume is smaller. Refinement of the structure by the method of restrained least squares (current R = 0.175) permits the assignment of isotropic atomic mean-square displacements to all nonhydrogen atoms. Comparison with the values obtained earlier at 250-300 K indicates that the protein at 80 K is more rigid. The average experimentally determined Debye-Waller factor, B, for the protein is 14A2 at 300 K and 5A2 at 80 K. Plots of backbone mean-square displacement vs. temperature show a discontinuity of slope for at least one-third of all residues. This behavior is in good agreement with the temperature dependence of the mean-square displacement of the heme iron as measured by Mössbauer absorption. The magnitudes of the smallest mean-square displacements observed at 80 K indicate that intramolecular motions can be frozen out to a surprisingly large degree. Even at 80 K, however, some atoms in myoglobin still have mean-square displacements greater than 0.1A2, thus providing evidence for conformational substates.
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Cites
Hemoglobin and myoglobin in their reactions with ligands
Antonini, E., & Brunori, M. (1971) · Medical Entomology and Zoology · Cited by 2,671
Dynamics of ligand binding to myoglobin
Austin, R. H., Beeson, K. W., Eisenstein, L., Frauenfelder, H., & Gunsalus, I. C. (1975) · Biochemistry · doi:10.1021/bi00695a021 · Cited by 1,624
Self-citationTemperature-dependent X-ray diffraction as a probe of protein structural dynamics
Frauenfelder, H., Petsko, G. A., & Tsernoglou, D. (1979) · Nature · doi:10.1038/280558a0 · Cited by 1,149
Self-citationStructure of myoglobin refined at 2·0 Å resolution
Takano, T. (1977) · Journal of Molecular Biology · doi:10.1016/s0022-2836(77)80111-3 · Cited by 676
Solvent viscosity and protein dynamics
Beece, D., Eisenstein, L., Frauenfelder, H., Good, D., Marden, M. C., Reinisch, L., Reynolds, A. H., Sorensen, L. B., & Yue, K. T. (1980) · Biochemistry · doi:10.1021/bi00564a001 · Cited by 669
Self-citationThe Internal Dynamics of Globular Protein
Karplus, M., McCammon, J. A., & Peticolas, W. L. (1981) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238109105437 · Cited by 511
Crystallographic studies of the dynamic properties of lysozyme
Artymiuk, P. J., Blake, C. C. F., Grace, D. E. P., Oatley, S. J., Phillips, D. C., & Sternberg, M. J. E. (1979) · Nature · doi:10.1038/280563a0 · Cited by 438
Packing of α-helices: Geometrical constraints and contact areas
Richmond, T. J., & Richards, F. M. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90201-2 · Cited by 363
Dynamics of metmyoglobin crystals investigated by nuclear gamma resonance absorption
Parak, F., Frolov, E. N., Mössbauer, R. L., & Goldanskii, V. I. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90317-x · Cited by 226
Self-citationDynamics of a protein matrix revealed by fluorescence quenching.
Eftink, M. R., & Ghiron, C. A. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.9.3290 · Cited by 156
Cited by
The Energy Landscapes and Motions of Proteins
Frauenfelder, H., Sligar, S. G., & Wolynes, P. G. (1991) · Science · doi:10.1126/science.1749933 · Cited by 3,250
Self-citationHarmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor.
Brooks, B., & Karplus, M. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.21.6571 · Cited by 829
Unusual biophysics of intrinsically disordered proteins
Uversky, V. N. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.12.008 · Cited by 566
Clore, G. M., Driscoll, P. C., Wingfield, P. T., & Gronenborn, A. M. (1990) · Biochemistry · doi:10.1021/bi00484a006 · Cited by 437
Rebinding and relaxation in the myoglobin pocket
Ansari, A., Berendzen, J., Braunstein, D., Cowen, B. R., Frauenfelder, H., Hong, M. K., Iben, I. E. T., Johnson, J. B., Ormos, P., Sauke, T. B., et al. (1987) · Biophysical Chemistry · doi:10.1016/0301-4622(87)80034-0 · Cited by 356
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Metadata
- Authors
- Hartmann, H., Parak, F., Steigemann, W., Petsko, G. A., Ponzi, D. R., & Frauenfelder, H.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1982-08
- Volume
- 79
- Issue
- 16
- Pages
- 4967-4971
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2026513163
- Cited by
- 254
- References
- 13
- FWCI
- 5.57
- Type
- journal article
- Language
- en
- Open access
- green
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- Hartmann, H., Parak, F., Steigemann, W., Petsko, G. A., Ponzi, D. R., & Frauenfelder, H. (1982). Conformational substates in a protein: structure and dynamics of metmyoglobin at 80 K. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.79.16.4967
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