Description

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

@introbul:Key Features @bul:* Molecular structure and dynamics * Spectroscopy * Ligand binding * Mathematical analysis and modeling

Readership

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.

Table of Contents

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 Protei

Details

No. of pages:
725
Language:
English
Copyright:
© 1994
Published:
Imprint:
Academic Press
Electronic ISBN:
9780080883458
Print ISBN:
9780121821333

About the serial-volume-editors

Reviews

@from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for biochemists." @source:--JOURNAL OF CHROMATOGRAPHY