Hemoglobins, Part C Biophysical Methods

✍ Scribed by Johannes Everse, Kim D. Vandegriff, Robert M. Winslow

• Publisher: Academic Press
• Year: 1994
• Tongue: English
• Leaves: 752
• Series: Methods in Enzymology 232
• Edition: 1
• Category: Library

✦ Synopsis

Hemoglobin has been involved in the most significant advances in our understanding of modern genetics and molecular biology. Now, hemoglobin is again central to a new area: Development of artificial blood (blood substitute.)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. Key Features Molecular structure and dynamics Spectroscopy Ligand binding Mathematical analysis and modeling

✦ Table of Contents

Contributors to Volume 232......Page 2
Preface......Page 5
Volume In Series......Page 7
[1] Acid-induced folding of heme proteins......Page 21
[2] X-ray crystallography of partially liganded structures......Page 34
[3] Structure and energy change in hemoglobin by hydrogen exchange labeling......Page 46
[4] High-pressure fluorescence methods for observing subunit dissociation in hemoglobin......Page 63
[5] Optical measurements of quaternary structural changes in hemoglobin......Page 77
[6] Allosteric equilibrium measurements with hemoglobin valency hybrids......Page 93
[7] Electron-transfer reactions of hemoglobin with small molecules A potential probe of conformational dynamics......Page 109
[8] Proton nuclear magnetic resonance studies of hemoglobin......Page 118
[9] Infrared methods for study of hemoglobin reactions and structures......Page 161
[10] Picosecond infrared spectroscopy of hemoglobin and myoglobin......Page 198
[11] Time-resolved resonance raman spectroscopy as probe of structure, dynamics, and reactivity in hemoglobin......Page 227
[12] Front-face fluorescence spectroscopy of hemoglobins......Page 254
[13] Stationary and time-resolved circular dichroism of hemoglobins......Page 270
[14] X-ray absorption spectroscopy of hemoglobin......Page 290
[15] Modulated excitation spectroscopy in hemoglobin......Page 317
[16] Picosecond phase grating spectroscopy applications to bioenergetics and protein dynamics......Page 347
[17] Assignment of rate constants for O2 and CO binding to α and β subunits within R- and T-state human hemoglobin......Page 386
[18] Ligand binding and conformational changes measured by time-resolved absorption spectroscopy......Page 410
[19] Femtosecond measurements of geminate recombination in heme proteins......Page 439
[20] Double mixing methods for kinetic studies of ligand binding in partially liganded intermediates of hemoglobin......Page 454
[21] Hemoglobin-liganded intermediates......Page 470
[22] Hemoglobin-oxygen equilibrium binding Rapid-scanning spectrophotometry and singular value decomposition......Page 486
[23] Oxygen equilibrium curve of concentrated hemoglobin......Page 512
[24] Bezafibrate derivatives as potent effectors of hemoglobin......Page 522
[25] Simulation of hemoglobin kinetics using finite element numerical methods......Page 540
[26] Adair fitting to oxygen equilibrium curves of hemoglobin......Page 582
[27] Weighted nonlinear regression analysis of highly cooperative oxygen equilibrium curves......Page 600
[28] Dimer-tetramer equilibrium in Adair fitting......Page 622
[29] Effects of wavelength on fitting Adair constants for binding of oxygen to human hemoglobin......Page 632
[30] Adair equation Rederiving oxygenation parameters......Page 659
[31] Linkage thermodynamics......Page 683
Author Index......Page 712
Subject Index......Page 735