The Use of High-Pressure Nuclear Magnetic Resonance to Study Protein Folding

  • Michael W. Lassalle
  • Kazuyuki Akasaka
Part of the Methods in Molecular Biology™ book series (MIMB, volume 350)


Recent development of high-pressure cells for a variety of spectroscopic methods has enabled the use of pressure as one of the commonly used perturbations along with temperature and chemical perturbations to study folding/unfolding reactions of proteins. Although various high-pressure spectroscopy techniques have their own significance, high-pressure nuclear magnetic resonance (NMR) is unique in that it allows one to gain residue-specific and atom-detailed information from proteins under pressure. Furthermore, because of a peculiar volume property of a protein, high-pressure NMR allows one to obtain structural information of a protein in a wide conformational space from the bottom to the upper region of the folding funnel, giving structural reality for the “open” state of a protein proposed from hydrogen exchange. The method allows a link between equilibrium folding intermediates and the kinetic intermediates, and manifests a new view of proteins as dynamic entities amply fluctuating among the folded, intermediate, and unfolded sub ensembles. This chapter briefly summarizes the technique, the principle, and the ways to use high-pressure NMR for studying protein folding.

Key Words

Pressure protein folding thermodynamic stability volume change structures of folding intermediates high-pressure NMR pressure-jump 


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Copyright information

© Humana Press Inc. 2007

Authors and Affiliations

  • Michael W. Lassalle
    • 1
  • Kazuyuki Akasaka
    • 2
  1. 1.Exploratory Research for Advanced Technology “Actin Filament Dynamics” ProjectJapan Science and Technology CorporationHyogoJapan
  2. 2.Department of Biotechnological Science, School of Biology-Oriented Science and TechnologyKinki UniversityKinokawa City, Wakayama PrefectureJapan

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