Fluorescence SpectroscopyEdited by
- Ludwig Brand
- Michael Johnson
- John Abelson
- Melvin Simon
The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. More than 270 volumes have been published (all of them still in print) and much of the material is relevant even today--truly an essential publication for researchers in all fields of life sciences.
Biochemists, biophysicists, cell biologists, and molecular biologists.
Methods in Enzymology
Hardbound, 628 Pages
Published: May 1997
Imprint: Academic Press
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- G. Weber, Fluorescence in Biophysics: Accomplishments and Deficiencies. B.Z. Packard, D.D. Toptygin, A. Komoriya, and L. Brand, Design of Profluorescent Protease Substrates Guided by Exciton Theory. J.M. Beechem, Picosecond Fluorescence Decay Curves Collected on Millisecond Time Scale: Direct Measurement of Hydrodynamic Radii, Local/Global Mobility, and Intramolecular Distances during Protein Folding Reactions. J.A. Schauerte, D.G. Steel, and A. Gafni, Time-Resolved Room Temperature Tryptophan Phosphorescence in Proteins. J.M. Vanderkooi, P.J. Angiolillo, and M. Laberge, Fluorescence Line Narrowing Spectroscopy: A Tool for Studying Proteins. A. Kowalczyk, N. Boens, and M. Ameloot, Determination of Ground-State Dissociation Constant by Fluorescence Spectroscopy. P.R. Callis, 1La and 1Lb Transitions of Tryptophan: Applications of Theory and Experimental Observations to Fluorescence of Proteins. J.B.A. Ross, A.G. Szabo, and C.W.V. Hogue, Enhancement of Protein Spectra with Tryptophan Analogues: Fluorescence Spectroscopy of ProteinâProtein and ProteinâNucleic Acid Interactions. M.D. Barkley and M.L. McLaughlin, Time-Resolved Fluorescence of Constrained Tryptophan Derivatives: Implications for Protein Fluorescence. T.E.S. Dahms and A.G. Szabo, Conformational Heterogeneity in Crystalline Proteins: Time-Resolved Fluorescence Studies. M.R. Eftink, Fluorescence Methods for Studying Equilibrium Macromolecule-Ligand Interactions. M.R. Eftink and M.C.R. Shastry, Fluorescence Methods for Studying Kinetics of Protein Folding Reactions. S.S. Lehrer, Intramolecular Pyrene Excimer Fluorescence: A Probe of Proximity and Protein Conformational Change. E. Terpetschnig, H. Szmacinski, and J.R. Lakowicz, Long Lifetime Metal-Ligand Complexes as Probes in Biophysics and Clinical Chemistry. P. Wu and L. Brand, N-Terminal Modification of Proteins for Fluorescence Measurements. P.S. Eis, Fluorescence Studies of Zinc Finger Peptides and Proteins. S.P. Lee and M.K. Han, Fluorescence Assays for DNA Cleavage. D.M. Jameson and J.F. Eccleston, Fluorescent Nucleotide Analogs: Synthesis and Applications. J.J. Hill and C.A. Royer, Fluorescence Approaches to Study of Protein-Nucleic Acid Complexation. M. Yang and D.P. Millar, Fluorescence Resonance Energy Transfer as Probe of DNA Structure and Function. J. Matko and M. Edidin, Energy Transfer Methods for Detecting Molecular Clusters on Cell Surfaces. A.S. Ladokhin, Distribution Analysis of Depth-Dependent Fluorescence Quenching in Membranes: A Practical Guide. A.S. Ladokhin, W.C. Wimley, K. Hristova, and S.H. White, Mechanism of Leakage of Contents of Membrane Vesicles Determined by Fluorescence Requenching. L. Davenport, Fluorescence Probes for Studying Membrane Heterogeneity. K.B. Lee and Y.C. Lee, Preparation of Bifluorescent-Labeled Glycopeptides for Glycoamidase Assay. K. Matsuoka, S.-I. Nishimura, and Y.C. Lee, Preparation of Fluorescent-Labeled Neoglycolipids for Ceramide Glycanase Assays. R.E. McCarty, Applications of Fluorescence Energy Resonance Transfer to Structure and Mechanism of Chloroplast ATPSynthase. Z. Gryczynski, J. Lubkowski, and E. Bucci, Intrinsic Fluorescence of Hemoglobins and Myoglobins. M.L. Johnson, Multiple-Domain Fluorescence Lifetime Data Analysis. Author Index. Subject Index.