Fluorescence studies of structural fluctuations in macromolecules as observed by fluorescence spectroscopy in the time, lifetime, and frequency domains.

Methods in enzymology ·Vol. 131 ·1986-00-00 ·Pages 518-67

Lakowicz JR

Abstract

Fluorescence spectroscopy provides numerous opportunities for determination of the dynamic properties of macromolecules. Measurements may be performed in the time, lifetime, or the frequency domain. Presently, the highest resolution is provided by the frequency-domain measurements, using the newly available instruments.

MeSH Terms

Kinetics Macromolecular Substances Protein Conformation Proteins/metabolism Solvents Spectrometry, Fluorescence/methods Time Factors Tryptophan

Chemicals

Macromolecular Substances Proteins Solvents Tryptophan

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Lakowicz J R

Article Info

Journal

Methods in enzymology

Abbr.

Methods Enzymol

ISSN

0076-6879

DOI

10.1016/0076-6879(86)31054-1

Published

1986-00-00

Pages

518-67

Language

English

Region

United States

NLM ID

0212271

Subset

External Links

PubMed source DOI: 10.1016/0076-6879(86)31054-1 View journal details

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Fluorescence studies of structural fluctuations in macromolecules as observed by fluorescence spectroscopy in the time, lifetime, and frequency domains.

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