Pressure-induced changes in the folded structure of lysozyme.
We demonstrate, for the first time in solution, that pressure induces changes in the overall folded structure of a protein (lysozyme). This was made possible by using a home-developed, on-line continuously variable pressure cell on a high resolution NMR spectrometer operating at 750 MHz. We could follow pressure-induced diamagnetic chemical shifts of more than 26 protons of lysozyme at variable pressure in the range of 1 to 2000 bar. The results indicate that the main effect of the pressure is a compaction of the hydrophobic core part of the protein consisting of bulky side-chains. The technique introduced here provides a general method with which one can probe microscopic internal flexibility of a protein in solution.
Akasaka
K
K
The Graduate School of Science and Technology, Kobe University, 1-1 Rokkodai-cho, Kobe, Nada-ku, 657, Japan.
Tezuka
T
T
Yamada
H
H
D000818:Animals; D002021:Buffers; D002645:Chickens; D005998:Glycine; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy / Q000295:instrumentation*; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry*; D011312:Pressure; D017510:Protein Folding
D002021:Buffers; D009113:Muramidase; D005998:Glycine