Hemoglobins: Hemoglobins, Part C: Biophysical Methods Biophysical Methods: Pt. C Volume 232
This volume of Methods in Enzymology and its companion Volume 231 are indispensable to anyone with a serious interest in this emerging field. They completely updated and extended the information presented in Volume 76, which was published more than 10 years ago.
- Hardback | 725 pages
- 158 x 226 x 38mm | 1,179.35g
- 24 May 1994
- Elsevier Science Publishing Co Inc
- Academic Press Inc
- San Diego, United States
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Table of contents
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.
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.