Protein conformation monitored by energy-selective optical spectroscopy

Jane M. Vanderkooi, A. Kaposi, J. Fidy

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Fluctuations in the polypeptide chain lead to disorder in proteins and to a distribution in the parameters that regulate their functions. Using low temperature (to reduce the fluctuations) and narrow-band lasers (to select one substrate among the many forms), high-resolution absorption and fluorescence spectra for chromophores in proteins can be obtained. These spectra reveal information on the kind and extent of disorder in proteins and allow for the determination of the vibrational energies of both ground and excited state molecules, true inhomogeneous spectral width, and kinetic studies of individual protein substrates.

Original languageEnglish
Pages (from-to)71-76
Number of pages6
JournalTrends in Biochemical Sciences
Volume18
Issue number3
DOIs
Publication statusPublished - 1993

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Protein Conformation
Conformations
Spectrum Analysis
Proteins
Substrates
Chromophores
Excited states
Ground state
Lasers
Fluorescence
Peptides
Molecules
Kinetics
Temperature
Optical spectroscopy

ASJC Scopus subject areas

  • Biochemistry

Cite this

Protein conformation monitored by energy-selective optical spectroscopy. / Vanderkooi, Jane M.; Kaposi, A.; Fidy, J.

In: Trends in Biochemical Sciences, Vol. 18, No. 3, 1993, p. 71-76.

Research output: Contribution to journalArticle

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