Pressure-tuning the conformation of bovine pancreatic trypsin inhibitor studied by Fourier-transform infrared spectroscopy

K. Goossens, L. Smeller, J. Frank, K. Heremans

Research output: Article

69 Citations (Scopus)

Abstract

A hydrostatic pressure of 1.5 GPa induces changes in the secondary structure of bovine pancreatic tryspin inhibitor (BPTI) as revealed by the analysis of the amide I' band with Fourier-transform infrared (FTIR) spectroscopy in the diamond anvil cell. The features of the secondary structure remain distinct at high pressure suggesting that the protein does not unfold. The fitted percentages of the secondary structure elements during compression and decompression strongly suggest that the pressure-induced changes are reversible. The pressure-induced changes in the tyrosine side chain band are also reversible. The results demonstrate that the infrared technique explores different aspects of the behaviour of proteins in comparison with two published molecular dynamics studies performed up to 1 GPa [Kitchen, D. B., Reed, L. H. and Levy, R. M. (1992) Biochemistry 32, 10083-10093] and 509 MPa [Brunne, R. M. and van Gunsteren, W. E (1993) FEES Lett. 323, 215-217]. A possible explanation for the difference is the time scale of the experiments.

Original languageEnglish
Pages (from-to)254-262
Number of pages9
JournalEuropean Journal of Biochemistry
Volume236
Issue number1
Publication statusPublished - 1996

Fingerprint

Aprotinin
Fourier Transform Infrared Spectroscopy
Conformations
Tuning
Pressure
Biochemistry
Diamond
Hydrostatic Pressure
Hydrostatic pressure
Molecular Dynamics Simulation
Decompression
Amides
Tyrosine
Molecular dynamics
Proteins
Infrared radiation
Experiments

ASJC Scopus subject areas

  • Biochemistry

Cite this

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title = "Pressure-tuning the conformation of bovine pancreatic trypsin inhibitor studied by Fourier-transform infrared spectroscopy",
abstract = "A hydrostatic pressure of 1.5 GPa induces changes in the secondary structure of bovine pancreatic tryspin inhibitor (BPTI) as revealed by the analysis of the amide I' band with Fourier-transform infrared (FTIR) spectroscopy in the diamond anvil cell. The features of the secondary structure remain distinct at high pressure suggesting that the protein does not unfold. The fitted percentages of the secondary structure elements during compression and decompression strongly suggest that the pressure-induced changes are reversible. The pressure-induced changes in the tyrosine side chain band are also reversible. The results demonstrate that the infrared technique explores different aspects of the behaviour of proteins in comparison with two published molecular dynamics studies performed up to 1 GPa [Kitchen, D. B., Reed, L. H. and Levy, R. M. (1992) Biochemistry 32, 10083-10093] and 509 MPa [Brunne, R. M. and van Gunsteren, W. E (1993) FEES Lett. 323, 215-217]. A possible explanation for the difference is the time scale of the experiments.",
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AU - Goossens, K.

AU - Smeller, L.

AU - Frank, J.

AU - Heremans, K.

PY - 1996

Y1 - 1996

N2 - A hydrostatic pressure of 1.5 GPa induces changes in the secondary structure of bovine pancreatic tryspin inhibitor (BPTI) as revealed by the analysis of the amide I' band with Fourier-transform infrared (FTIR) spectroscopy in the diamond anvil cell. The features of the secondary structure remain distinct at high pressure suggesting that the protein does not unfold. The fitted percentages of the secondary structure elements during compression and decompression strongly suggest that the pressure-induced changes are reversible. The pressure-induced changes in the tyrosine side chain band are also reversible. The results demonstrate that the infrared technique explores different aspects of the behaviour of proteins in comparison with two published molecular dynamics studies performed up to 1 GPa [Kitchen, D. B., Reed, L. H. and Levy, R. M. (1992) Biochemistry 32, 10083-10093] and 509 MPa [Brunne, R. M. and van Gunsteren, W. E (1993) FEES Lett. 323, 215-217]. A possible explanation for the difference is the time scale of the experiments.

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KW - Bovine pancreatic trypsin inhibitor

KW - High pressure

KW - Infrared spectroscopy

KW - Molecular dynamics

KW - Protein unfolding

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