Hemoglobins, Part C: Biophysical Methods, 232
- Johannes Everse, School of Medicine, Texas Tech University Health Science Center, Lubbock, U.S.A.
- Kim Vandegriff, University of California, Department of Medicine and Veterans Affairs Medical Center, San Diego, U.S.A.
- John Abelson, California Institute of Technology, Division of Biology, Pasadena, U.S.A.
- Melvin Simon, California Institute of Technology, Division of Biology, Pasadena, U.S.A.
Biochemists, molecular biologists, cell biologists, physiologists, pathologists, biophysicists, clinical chemists, industrial and academic researchers involved in the preparation of hemoglobin derivatives and in the preparationand analysis of recombinant proteins.
Methods in Enzymology
Published: April 1994
Imprint: Academic Press
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- Molecular Structure and Dynamics:Y. Goto and A.L. Fink, Acid-Induced Folding of Heme Proteins.R. Liddington, X-Ray Crystallography of Partially Liganded Structures.S.W. Englander and J.J. Englander, Structure and Energy Change in Hemoglobin by Hydrogen Exchange Labeling.S. Pin and C.A. Royer, High-Pressure Fluorescence Methods for Observing Subunit Dissociation in Hemoglobin.A. Bellelli and M. Brunori, Optical Measurements of QuaternaryStructural Changes in Hemoglobin.M.C. Marden, J. Kister, and C. Poyart, Allosteric Equilibirum Measurements with Hemoglobin Valency Hybrids.G. McLendon and J. Feitelson,Electron-Transfer Reactions of Hemoglobin with Small Molecules: A Potential Probe of Conformational Dynamics. Spectroscopy:C. Ho and J.R. Perussi, Proton Nuclear Magnetic Resonance Studies of Hemoglobin.A. Dong and W.S. Caughey, Infrared Methods for Study of Hemoglobin Reactions and Structures.R. H. Austin and L. J. Rothberg, Picosecond Infrared Spectroscopy of Hemoglobin and Myoglobin.J.M. Friedman, Time-Resolved Resonance Raman Spectroscopy as Probe of Structure, Dynamics, and Reactivity in Hemoglobin.R.E. Hirsch, Front-Face Fluorescence Spectroscopy of Hemoglobins.C. Zentz, S. Pin, and B. Alpert, Stationary and Time-Resolved Circular Dichroism of Hemoglobins.S. Pin, B. Alpert, A. Congiu-Castellano, S.D. Longa, and A. Bianconi, X-Ray Absorption Spectroscopy of Hemoglobin.F.A. Ferrone, Modulated Excitation Spectroscopy in Hemoglobin.J. Deak, L. Richard, M. Pereira, H.-L. Chui, and R.J.D. Miller, Picosecond Phase Grating Spectroscopy: Applications to Bioenergetics and Protein Dynamics.Ligand Binding:A.J. Mathews and J.S. Olson, Assignment of Rate Constants for O2 and CO Binding to a and b Subunits within R- and T-State Human Hemoglobin.J. Hofrichter, A. Ansari, C.M. Jones, R.M. Deutsch, J.H. Sommer, and E.R. Henry, Ligand Binding and Conformational Changes Measured by Time-Resolved Absorption Spectroscopy.J.-L. Martin and M.H. Vos, Femtosecond Measurements of Geminate Recombination in Heme Proteins.V.S. Sharma, Double Mixing Methods for Kinetic Studies of Ligand Binding inPartially Liganded Intermediates of Hemoglobin.M. Perrella and L. Rossi-Bernardi, Hemoglobin-Liganded Intermediates.K.D. Vandegriff and R.I. Shrager, Hemoglobin-Oxygen Equilibrium Binding: Rapid-Scanning Spectrophotometry and Singular Value Decomposition.R.M. Winslow, A. Murray, and C.C. Gibson, Oxygen Equilibrium Curve of Concentrated Hemoglobin.C. Poyart, M.C. Marden, and J. Kister, Bezafibrate Derivatives as Potent Effectors of Hemoglobin.Mathematical Analysis and Modeling:R.L. Berger, N. Davids, and M. Perrella, Simulation of Hemoglobin Kinetics Using Finite Element Numerical Methods.K. Imai, Adair Fitting to Oxygen Equilibrium Curves of Hemoglobin.M.L. Doyle, D.W. Myers, G.K. Ackers, and R. I. Shrager, Weighted Nonlinear Regression Analysis of Highly Cooperative Oxygen Equilibrium Curves.M.L. Johnson, Dimer-Tetramer Equilibrium in Adair Fitting.L. J. Parkhurst, T.M. Larsen, and H.-Y. Lee, Effects of Wavelength on Fitting Adair Constants for Binding of Oxygen to Human Hemoglobin.E.C. DeLand, Adair Equation: Rederiving Oxygenation Parameters.E. Di Cera, Linkage Thermodynamics.Author Index.Subject Index.