Biochemical spectroscopy

Bibliographic Information

Biochemical spectroscopy

edited by Kenneth Sauer

(Methods in enzymology / editors in chief, Sidney P. Colowick, Nathan O. Kaplan, v. 246)

Academic Press, c1995

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Includes bibliographical references and indexes

Description and Table of Contents

Description

This volume includes spectroscopic methods for the characterization of macromolecules. Methods span the electromagnetic spectrum from X-ray to microwaves. It focuses on the types of information that can be derived: how measurements are made; state of the art apparatus; data acquisition, analysis, and interpretation; casebook examples; and new developments and future directions.

Table of Contents

K. Sauer, Why Spectroscopy? Which Spectroscopy? Ultraviolet/Visible Spectroscopy: I. Tinoco, Jr., Optical Spectroscopy: General Principles and Overview. A. Absorption and Circular Dichroism: D.M. Gray, S.-H. Hung, and K.H. Johnson, Absorption and Circular Dichroism Spectroscopy of Nucleic Acid Duplexes and Triplexes. R.W. Woody, Circular Dichroism. E.I. Solomon, M.L. Kirk, D.R. Gamelin, and S. Pulver, Bioinorganic Spectroscopy. J.C.Sutherland, Magnetic Circular Dichroism. R.H. Austin and S. Erramilli, Low-Temperature Spectroscopy. B. Transient Absorption and Kinetics: P.S. Brzovic and M.F. Dunn, Rapid-Scanning Ultraviolet/Visible Spectroscopy Applied in Stopped-Flow Studies. H. van Amerongen and R. van Grondelle, Transient Absorption Spectroscopy in Study of Processes and Dynamics in Biology. J. Friedrich, Hole Burning Spectroscopy and Physics of Proteins. C. Linear Dichroism and Fluorescence: H. van Amerongen and W.S. Struve, Polarized Optical Spectroscopy of Chromoproteins. D.M. Jameson and W.H. Sawyer, Fluorescence Anisotropy Applied to Biomolecular Interactions. P.R. Selvin, Fluorescence Resonance Energy Transfer. A.R. Holzwarth, Time-Resolved Fluorescence Spectroscopy. A. Waggoner, Covalent Labeling of Proteins and Nucleic Acids with Fluorophores. Vibrational Spectroscopy: R.A. Mathies, Biomolecular Vibrational Spectroscopy. W.L.Peticolas, Raman Spectroscopy of DNA and Proteins. T.G. Spiro and R.S. Czernuszewicz, Resonance Raman Spectroscopy of Metalloproteins. J.R. Kincaid, Structure and Dynamics of Transient Species Using Time-Resolved Resonance Raman Spectroscopy. F. Siebert, Infrared Spectroscopy Applied to Biochemical and Biological Problems. Magnetic Resonance Spectroscopy, X-Ray Spectroscopy: M.P. Klein, Perspectives on Magnetic Resonance and X-Ray Absorption Spectroscopy in Biochemistry. G.W. Brudvig, Electron Paramagnetic Resonance Spectroscopy. V.J. DeRose and B.M. Hoffman, Protein Structure and Mechanism Studied by Electron Nuclear Double Resonance Spectroscopy. G.L. Millhauser, W.R. Fiori, and S.M. Miick, Electron Spin Labels. A.H. Maki, Optically Detected Magnetic Resonance of Photoexcited Triplet States. V.K. Yachandra, X-Ray Absorption Spectroscopy and Applications in Structural Biology. Special Topics: R.T. Ross and S. Leurgans, Component Resolution Using Multilinear Models. S. Dong, J. Niu, and T.M. Cotton, Ultraviolet/Visible Spectroelectrochemistry of Redox Proteins. D.C. Youvan, E. Goldman, S. Delagrave, and M.M. Yang, Digital Imaging Spectroscopy for Massively Parallel Screening of Mutants. H. Scheer, Diode Array Detection in Liquid Chromatography. Author Index. Subject Index.

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  • Methods in enzymology

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    Academic Press c1955-

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    Available at 179 libraries

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