Fluorescence Spectroscopy / Edition 1

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Fluorescence spectroscopy is a type of electromagnetic spectroscopy, using a beam of light, which analyzes fluorescence from a sample. Given its extremely high sensitivity and selectivity, it is an important investigational tool in many areas including material sciences, analytical sciences, and across a broad range of chemical, biochemical and medical research. It has become an essential investigational technique allowing detailed, real-time observation of the structure and dynamics of intact biological systems. The pharmaceutical industry uses it heavily and it has become a dominating technique in biochemistry and molecular genetics.

• Keeps MIE buyers and online subscribers up-to-date with the latest research with this highly used technique.

• Provides tried and tested techniques which eliminate searching through many different sources.

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Editorial Reviews

Doody's Review Service
Reviewer: Howard H. Sky-Peck, MD, PhD, FRSM (Rush Medical College of Rush University)
Description: The Methods in Enzymology series has been an important reference collection in libraries for many years. Volume 278 on fluorescence spectroscopy is no exception. It is a detailed description of the state of advancement and methodology.
Purpose: There have been significant advances in instrumentation, particularly in regard to time-resolved measurements and procedures for data analysis. More information on intrinsic fluorescent probes, such as tryptophan, have become available, and new types of probes and ways of attaching them to macromolecules have been described. It is now possible to do nanosecond time-resolved measurements through a microscope.
Audience: The volume is intended for scientific practitioners who wish to become acquainted with this methodology and have the necessary background.
Features: Topics covered in this volume include discussions of the fluorescence of tryptophan, the origin of the excited states, and their sensitivity to environmental perturbations. Studies of constrained tryptophan residues have been helpful in this regard. The fluorescence of proteins can be used to study equilibria and kinetics of protein-protein and protein-nucleic acid interaction. New technology is described that allows fluorescence lifetimes to be used to study slower kinetic processes. Fluorescence also provides excellent ways to measure DNA cleavage.
Assessment: This volume is designed as a means of acquainting bioscientists with the up-to-date uses and the importance of fluorescence spectroscopy in the analysis of macromolecules. It accomplishes these objectives very well and should be included in science libraries.
From the Publisher
Praise for the Series
"The Methods in Enzymology series represents the gold-standard."
"Incomparably useful."
"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."
"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."
"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."
"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."
"A series that has established itself as a definitive reference for biochemists."
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Product Details

  • ISBN-13: 9780121821791
  • Publisher: Elsevier Science
  • Publication date: 5/1/1997
  • Series: Methods in Enzymology Series
  • Edition number: 1
  • Pages: 660
  • Product dimensions: 1.63 (w) x 6.00 (h) x 9.00 (d)

Table of Contents

Direct quantitation of Mg2+ - RNA interactions use of a fluorescent dye
Dan Grilley, Ana Maria Soto, and David E. Draper

A Method in Enzymology for Measuring Intracellular Protease Activities in Live Cells
Beverly Z. Packard and Akira Komoriya

Using Fluorophore-labeled Oligonucleotides to Measure Affinities of Protein-DNA Interactions
Brian J. Anderson and Joel F. Schildbach

Site-Selective Red-Edge Effects
Alexander P. Demchenko

Multiparametric Probing of Microenvironment with Solvatochromic Fluorescent Dyes Andrey S. Klymchenko and Alexander Demchenko

Pteridine Probes for Nucleic Acid Analysis
Mary E. Hawkins

Application of Single Molecule Spectroscopy in Studying Enzyme Kinetics and Mechanism Jue Shi, Ari Gafni, and Duncan Steel

Fluorescence Approaches in Quantifying Bio-Molecular Interactions
Catherine A. Royer and Suzanne

Applications of Up-Conversion Methods in Studies of Proteins and Peptides
Jay Knutson

Spectroscopic Studies of Molecular Solvent Relaxation
Mark Maroncelli

Single Molecule Fluorescence Studies of the Dynamics of Gene Regulation
Jie Xiao

New Fluorescence Methods for Studies of Muscle Proteins
Robert E. Dale

Fluorescence Probes for Analysis of Membrane Proteins
Amitabha Chattopadhyay

Fluorescence Methods for Protein-Protein interaction in Membranes
Kalina Hristova

Fluorescence Detection of Specific Ions
Bernard Valeur

Measuring Picomolar Intracellular Exchangable Zn in PC-12 Cells using a Ratiometric Fluorescence Biosensor
R.A. Bozym

Monitoring Free Zinc in the Mitochondrion
Richard B Thompson, et al

Metal-enhanced fluorescence: An emerging tool in biotechnology
Chris D. Geddes, et al

Radiative Decay Engineering, Surface Plasmon-Coupled Directional Emission
Joseph R Lakowicz, et al

Time-resolved fluorescence anisotropy and the measurement of protein conformational flexibility
David A. Johnson (University of California Riverside)

Tranes and other new Analysis Procedures in wavelength resolved fluorescence.
Pariasamy (Mumbay)

From Quantum Theory to Molecular Fluorescence.
D. Toptygin

Probing Protein Electrostatics with Synthetic amino acids.
Bruce Cohen (UCSF)

Analysis of Complex Fluorescence Anisotropy Decay
William Laws, Montana

Studies of Segmental Protein Dynamics with Time and Energy Resolved Fluorescence Spectroscopy
D. Toptygin and L. Brand

Complex Fluorescence Decay of Trytophan in Proteins.
Mary D. Barkley

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