Protein states and proteinquakes.

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 1,626 · see citing works

Temperature-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 1,151 · see citing works

Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale

Lakowicz, J. R., & Weber, G. (1973) · Biochemistry · doi:10.1021/bi00745a021 · Cited by 804 · see citing works

Structure and refinement of oxymyoglobin at 1·6 Å resolution

Phillips, S. E. V. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90262-4 · Cited by 645 · see citing works

Hemoglobin: Structure, function, evolution, and pathology

Brunori, M. (1984) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(84)90080-x · Cited by 509 · see citing works

Thermodynamic fluctuations in protein molecules.

Cooper, A. J. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.8.2740 · Cited by 411 · see citing works

Structural domains in proteins and their role in the dynamics of protein function

Janin, J., & Wodak, S. J. (1983) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(83)90003-2 · Cited by 283 · see citing works

Structural and Functional Aspects of Domain Motions in Proteins

Bennett, W. S., Huber, R., & Engel, J. (1984) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238409117796 · Cited by 245 · see citing works

Dynamics of metmyoglobin crystals investigated by nuclear gamma resonance absorption

Parak, F., Frolov, E. N., Mössbauer, R. L., et al. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90317-x · Cited by 226 · see citing works

[16] Polarized absorption and linear dichroism spectroscopy of hemoglobin

Eaton, W. A., & Hofrichter, J. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(81)76126-3 · Cited by 195 · see citing works

Femtosecond photolysis of CO-ligated protoheme and hemoproteins: appearance of deoxy species with a 350-fsec time constant.

Martin, J. L., Migus, A., Poyart, C., et al. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.1.173 · Cited by 192 · see citing works

Frontiers of Biological Energetics

(1978) · Elsevier eBooks · doi:10.1016/b978-0-12-225402-4.x5001-3 · Cited by 185 · see citing works

Hemoglobin tertiary structural change on ligand binding its role in the co-operative mechanism

Gelin, B. R., Lee, A. W.-M., & Karplus, M. (1983) · Journal of Molecular Biology · doi:10.1016/0022-2836(83)90042-6 · Cited by 172 · see citing works

A consistent picture of protein dynamics.

Parak, F., & Knapp, E. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.22.7088 · Cited by 159 · see citing works

Dynamics 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 155 · see citing works

A model of protein conformational substates

Stein, D. L. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.11.3670 · Cited by 151 · see citing works

Structure and motion: Membranes, nucleic acids and proteins

Fox, R. F. (1986) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(86)90048-4 · Cited by 144 · see citing works

Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobin.

Henry, E. R., Levitt, M., & Eaton, W. A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.7.2034 · Cited by 98 · see citing works

Low temperature photodissociation of hemoproteins: Carbon monoxide complex of myoglobin and hemoglobin

Iizuka, T., Yamamoto, H., Kotani, M., et al. (1974) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(74)90161-5 · Cited by 98 · see citing works

Dynamics of heme iron in crystals of metmyoglobin and deoxymyoglobin.

Bauminger, E. R., Cohen, S. G., Nowik, I., et al. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.3.736 · Cited by 88 · see citing works

The iron-proximal histidine linkage and protein control of oxygen binding in hemoglobin. A transient Raman study.

Friedman, J. M., Scott, T. W., Stepnoski, R. A., et al. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44493-0 · Cited by 81 · see citing works

Investigation of Large Intramolecular Movements within Metmyoglobin by Rayleigh Scattering of Mössbauer Radiation (RSMR)

Krupyanskiǐ, Y. F., Parak, F., Gol'danskiĭ, V. I., et al. (1982) · Zeitschrift für Naturforschung C · doi:10.1515/znc-1982-1-211 · Cited by 64 · see citing works

Low temperature photodissociation studies of ferrous hemoglobin and myoglobin complexes by Mössbauer spectroscopy

Spartalian, K., Lang, G., & Yonetani, T. (1976) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(76)90036-2 · Cited by 50 · see citing works

The physical aspects of energy transduction in biological systems

Blumenfeld, L. A. (1978) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500002286 · Cited by 46 · see citing works

Comparison of the magnetic properties of deoxy- and photodissociated myoglobin.

Röder, H., Berendzen, J., Bowne, S. F., et al. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.8.2359 · Cited by 35 · see citing works

Relaxation processes on a picosecond time scale in hemoglobin and poly( L ‐alanine) observed by millimeter‐wave spectroscopy

Genzel, L., Kremer, F., Poglitsch, A., & Bechtold, G. (1983) · Biopolymers · doi:10.1002/bip.360220708 · Cited by 35 · see citing works

Resonance Raman spectra of photodissociated carbonmonoxy hemoglobin and deoxy hemoglobin at 10 K.

Ondrias, M. R., Rousseau, D. L., & Simon, S. R. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)81940-1 · Cited by 28 · see citing works

A comparison of the heme electronic states in equilibrium and nonequilibrium protein conformations of high-spin ferrous hemoproteins low temperature magnetic circular dichroism studies

Sharonov, Y. A., Sharonova, N. A., Figlovsky, V. A., et al. (1982) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(82)90476-9 · Cited by 15 · see citing works

Reaction-rate theory: fifty years after Kramers

Hänggi, P., Talkner, P., & Borkovec, M. (1990) · Reviews of Modern Physics · doi:10.1103/revmodphys.62.251 · Cited by 6,154 · see citing works

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 · see citing works

Dynamic personalities of proteins

Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545 · see citing works

Ultrametricity for physicists

Rammal, R., Toulouse, G., & Virasoro, M. A. (1986) · Reviews of Modern Physics · doi:10.1103/revmodphys.58.765 · Cited by 756 · see citing works

Bulk-solvent and hydration-shell fluctuations, similar to α- and β-fluctuations in glasses, control protein motions and functions

Fenimore, P. W., Frauenfelder, H., McMahon, B. H., & Young, R. D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405573101 · Cited by 524 · see citing works

Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436 · see citing works

Ultrafast Spectroscopy: State of the Art and Open Challenges

Maiuri, M., Garavelli, M., & Cerullo, G. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b10533 · Cited by 460 · see citing works

The nature of folded states of globular proteins

Honeycutt, J. D., & Thirumalai, D. (1992) · Biopolymers · doi:10.1002/bip.360320610 · Cited by 360 · see citing works

Single-Molecule Fluorescence Spectroscopy of Photosynthetic Systems

Kondo, T., Chen, W. J., & Schlau-Cohen, G. S. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00195 · Cited by 120 · see citing works

Vibrational dynamics in the light-harvesting complexes of the photosynthetic bacterium Rhodobacter sphaeroides

Chachisvilis, M., Pullerits, T., Jones, M. R., Hunter, C. N., & Sundström, V. (1994) · Chemical Physics Letters · doi:10.1016/0009-2614(94)00560-5 · Cited by 118 · see citing works

Watching proteins function with time-resolved x-ray crystallography

Šrajer, V., & Schmidt, M. (2017) · Journal of Physics D: Applied Physics · doi:10.1088/1361-6463/aa7d32 · Cited by 67 · see citing works

Blue Myoglobin Reconstituted with an Iron Porphycene Shows Extremely High Oxygen Affinity

Hayashi, T., Dejima, H., Matsuo, T., et al. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0265052 · Cited by 124 · see citing works

Met-myoglobin formation, accumulation, degradation, and myoglobin oxygenation monitoring based on multiwavelength attenuance measurement in porcine meat

Nguyen, T. A., Kien, N. P., Lee, J.-B., et al. (2016) · Journal of Biomedical Optics · doi:10.1117/1.jbo.21.5.057002 · Cited by 13 · see citing works

The Diffusion Coefficient of Myoglobin in Muscle Homogenate

Oll, W. (1968)

A Histological Study of Myoglobin in Developing Muscle of the Pig

Morita, S., Cooper, C. C., CASSENS, R. G., et al. (1970) · Journal of Animal Science · doi:10.2527/jas1970.314664x · Cited by 7 · see citing works

The diffusion coefficient of myoglobin in muscle homogenate

Moll, W. (1968) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/bf00362587 · Cited by 39 · see citing works