Two-dimensional Fourier-transform infrared correlation spectroscopy study of the high-pressure tuning of proteins

L. Smeller, P. Rubens, J. Frank, J. Fidy, K. Heremans

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

2D FTIR gives new information about the pressure effect on the structure and dynamics of macromolecular systems. Application of this analysis to proteins can unravel the relation of conformational changes and H/D exchange processes. For lipoxygenase, a pressure of 6.5 kbar induces irreversible conformational changes resulting in an increased exposure of interior parts of the protein to the solvent. At the transition pressure the spectral changes indicate a correlation between conformational changes and H/D exchange. Below and above this pressure, the effects of H/D exchange on the spectral changes are predominant.

Original languageEnglish
Pages (from-to)119-125
Number of pages7
JournalVibrational Spectroscopy
Volume22
Issue number1-2
Publication statusPublished - 2000

Fingerprint

Fourier transforms
Tuning
Spectroscopy
Infrared radiation
Proteins
Pressure effects
Lipoxygenase

Keywords

  • FTIR correlation spectroscopy
  • H/D exchange
  • Proteins

ASJC Scopus subject areas

  • Analytical Chemistry
  • Spectroscopy

Cite this

Two-dimensional Fourier-transform infrared correlation spectroscopy study of the high-pressure tuning of proteins. / Smeller, L.; Rubens, P.; Frank, J.; Fidy, J.; Heremans, K.

In: Vibrational Spectroscopy, Vol. 22, No. 1-2, 2000, p. 119-125.

Research output: Contribution to journalArticle

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