Protein relaxation dynamics in human myoglobin

[1]  V. Šrajer,et al.  Investigations of optical line shapes and kinetic hole burning in myoglobin. , 1991, Biochemistry.

[2]  J. B. Johnson,et al.  Ligand binding to heme proteins: connection between dynamics and function. , 1991, Biochemistry.

[3]  Krzysztof Kuczera,et al.  Ligand binding and protein relaxation in heme proteins: a room temperature analysis of nitric oxide geminate recombination , 1991 .

[4]  J. Simon,et al.  Protein conformational relaxation following photodissociation of CO from carbonmonoxymyoglobin: picosecond circular dichroism and absorption studies. , 1991, Biochemistry.

[5]  R. Miller,et al.  Direct observation of global protein motion in hemoglobin and myoglobin on picosecond time scales. , 1991, Science.

[6]  Pál Ormos,et al.  Proteins and pressure , 1990 .

[7]  B. R. Cowen,et al.  Inhomogeneous broadening in spectral bands of carbonmonoxymyoglobin. The connection between spectral and functional heterogeneity. , 1990, Biophysical journal.

[8]  S. Boxer,et al.  Electrostatic interactions in wild-type and mutant recombinant human myoglobins. , 1989, Biochemistry.

[9]  Frauenfelder,et al.  Glassy behavior of a protein. , 1989, Physical review letters.

[10]  R. Hochstrasser,et al.  Picosecond transient absorption study of photodissociated carboxy hemoglobin and myoglobin. , 1988, Biophysical journal.

[11]  Lou Reinisch,et al.  Protein fluctuations, distributed coupling, and the binding of ligands to heme proteins , 1988 .

[12]  N Agmon,et al.  Reactive line-shape narrowing in low-temperature inhomogeneous geminate recombination of CO to myoglobin. , 1988, Biochemistry.

[13]  L. P. Murray,et al.  The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[14]  J. Westrick,et al.  A time-resolved photoacoustic calorimetry study of the dynamics of enthalpy and volume changes produced in the photodissociation of carbon monoxide from sperm whale carboxymyoglobin. , 1987, Biochemistry.

[15]  M R Chance,et al.  Linkage of functional and structural heterogeneity in proteins: dynamic hole burning in carboxymyoglobin. , 1987, Science.

[16]  D. Rousseau,et al.  Metastable photoproducts from carbon monoxide myoglobin. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[17]  R. Hochstrasser,et al.  Picosecond resonance Raman evidence for unrelaxed heme in the (carbonmonoxy)myoglobin photoproduct. , 1985, Biochemistry.

[18]  S. Boxer,et al.  Cloning, expression in Escherichia coli, and reconstitution of human myoglobin. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[19]  R D Young,et al.  Protein states and proteinquakes. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[20]  E. Henry,et al.  Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication. , 1985, Biochemistry.

[21]  J. Friedman,et al.  Picosecond time-resolved Raman studies of photodissociated carboxymyoglobin , 1985 .

[22]  J. Hopfield,et al.  CO binding to heme proteins: A model for barrier height distributions and slow conformational changes , 1983 .

[23]  E. Henry,et al.  Geminate recombination of carbon monoxide to myoglobin. , 1983, Journal of molecular biology.

[24]  E. Henry,et al.  Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[25]  H Frauenfelder,et al.  Control and pH dependence of ligand binding to heme proteins. , 1982, Biochemistry.

[26]  Richard I. Shrager,et al.  Titration of individual components in a mixture with resolution of difference spectra, pKs, and redox transitions , 1982 .

[27]  R. Stepnoski,et al.  Ligation and quaternary structure induced changes in the heme pocket of hemoglobin: a transient resonance Raman study. , 1982, Biochemistry.

[28]  J. Randall,et al.  Molecular dynamics of hydrated proteins , 1980 .

[29]  H Frauenfelder,et al.  Solvent viscosity and protein dynamics. , 1980, Biochemistry.

[30]  S. Phillips,et al.  Structure and refinement of oxymyoglobin at 1.6 A resolution. , 1980, Journal of molecular biology.

[31]  M. Karplus,et al.  Dynamics of ligand binding to heme proteins. , 1979, Journal of molecular biology.

[32]  C Chothia,et al.  Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism. , 1979, Journal of molecular biology.

[33]  B. Hasinoff.  The diffusion-controlled reaction kinetics of the binding of CO and O2 to myoglobin in glycerol-water mixtures of high viscosity. , 1977, Archives of biochemistry and biophysics.

[34]  T. Takano,et al.  Structure of myoglobin refined at 2-0 A resolution. I. Crystallographic refinement of metmyoglobin from sperm whale. , 1977, Journal of molecular biology.

[35]  H Frauenfelder,et al.  Dynamics of ligand binding to myoglobin. , 1975, Biochemistry.

[36]  B. Somogyi,et al.  Relationship between the lifetime of an enzyme-substrate complex and the properties of the molecular environment. , 1975, Journal of theoretical biology.

[37]  M. Perutz.  Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery , 1970, Nature.

[38]  M. Perutz,et al.  An x-ray study of azide methaemoglobin. , 1966, Journal of molecular biology.

[39]  R. G. Hart,et al.  Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution , 1960, Nature.

[40]  S. Carlill,et al.  Some observations on pulmonary haemodynamics in the cat , 1957, The Journal of physiology.

[41]  Q. Gibson.  An apparatus for flash photolysis and its application to the reactions of myoglobin with gases , 1956, The Journal of physiology.

[42]  Y. Lecarpentier,et al.  Femtosecond photolysis of CO-ligated protoheme and hemoproteins: appearance of deoxy species with a 350-fsec time constant. , 1983, Proceedings of the National Academy of Sciences of the United States of America.