2D FT-IR spectroscopy analysis of the pressure-induced changes in proteins

L. Smeller, K. Heremans

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

In this paper, we apply for the first time two-dimensional (2D) correlation spectroscopy to analyze pressure-induced changes in proteins. We show that it is possible to distinguish between hydrogen-deuterium (H/D) exchange and conformational changes from the synchronous and the asynchronous spectra. From the sequence of the spectral changes it can be concluded that the initial partial unfolding of the secondary structure enhances the exchange, which is followed by further conformational changes. The exchange process is complete below ca. 0.4 GPa. The elastic distortions of the protein at higher pressures seem not to be accompanied by H/D exchange.

Original languageEnglish
Pages (from-to)375-378
Number of pages4
JournalVibrational Spectroscopy
Volume19
Issue number2
Publication statusPublished - 1999

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Deuterium
Hydrogen
Infrared spectroscopy
Proteins
Spectroscopy

Keywords

  • FT-IR spectroscopy
  • Proteins
  • Two-dimensional (2D) correlation spectroscopy

ASJC Scopus subject areas

  • Analytical Chemistry
  • Spectroscopy

Cite this

2D FT-IR spectroscopy analysis of the pressure-induced changes in proteins. / Smeller, L.; Heremans, K.

In: Vibrational Spectroscopy, Vol. 19, No. 2, 1999, p. 375-378.

Research output: Contribution to journalArticle

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