Pressure‐Tuning the Conformation of Bovine Pancreatic Trypsin Inhibitor Studied by Fourier‐Transform Infrared Spectroscopy
作者： Koen Goossens , Laszlo Smeller , Johannes Frank , Karel Heremans
DOI: 10.1111/J.1432-1033.1996.00254.X
关键词:
摘要: A hydrostatic pressure of 1.5 GPa induces changes in the secondary structure bovine pancreatic tryspin inhibitor (BPTI) as revealed by analysis amide I' band with Fourier-transform infrared (FTIR) spectroscopy diamond anvil cell. The features remain distinct at high suggesting that protein does not unfold. fitted percentages elements during compression and decompression strongly suggest pressure-induced are reversible. tyrosine side chain also results demonstrate technique explores different aspects behaviour proteins comparison two published molecular dynamics studies performed up to 1 [Kitchen, D. B., Reed, L. H. & Levy, R. M. (1992) Biochemistry 31, 10083–10093] 500 MPa [Brunne, van Gunsteren, W. F. (1993) FEBS Lett. 323, 215–217]. possible explanation for difference is time scale experiments.
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