The effect of high pressure upon proteins and other biomolecules

Abstract

We shall not attempt here to enumerate the results or review in a systematic way the significant literature dealing with the use of high pressure in studies of proteins and other molecules of biological interest. Two recent reviews on this subject, one by MOrild (1981) and another by Heremans (1982), and a further article by Jaenicke (1981) on enzymes under extreme environmental conditions contain expositions and references that would render redundatn such a task. Rather we concentrate here on the examination of othe conceptual framework employed in the interpretation of high pressure experiments and in the critical discussion of our knowledge of selected areas of present interest and likely future significance.

Effects of pressure on the structure of metmyoglobin: Molecular dynamics predictions for pressure unfolding through a molten globule intermediate

“…Experimental techniques such as optical spectroscopy, Raman scattering, and NMR have been used to observe pressure effects on proteins (Weber & Drickamer, 1983;Frauenfelder et al, 1990;Jaenicke, 1991;Silva & Weber, 1993;Gross & Jaenicke, 1994 . The pressure denaturation of monomeric proteins, the dissociation of oligomers, and the effects of pressure on macromolecular assemblages have provided insights into the microscopic mechanism of protein folding and the role of solvent in this process (Zipp & Kauzmann, 1973;Li et al, 1976;Chryssomallis et al, 1981;Weber & Drickamer, 1983;Silva et al, 1986;Silva & Weber, 1993;Weber, 1993;Dufour et al, 1994;Peng et al, 1994;Schulte et al, 1995;Silva et al, 1996).…”

“…The pressure denaturation of monomeric proteins, the dissociation of oligomers, and the effects of pressure on macromolecular assemblages have provided insights into the microscopic mechanism of protein folding and the role of solvent in this process (Zipp & Kauzmann, 1973;Li et al, 1976;Chryssomallis et al, 1981;Weber & Drickamer, 1983;Silva et al, 1986;Silva & Weber, 1993;Weber, 1993;Dufour et al, 1994;Peng et al, 1994;Schulte et al, 1995;Silva et al, 1996). These effects are often reversible but can show different degrees of hysteresis.…”

Dissociation of peripheral protein‐membrane complexes by high pressure

“…This can be compared to the A E for dimerization of tryptophan synthase p2 (162 mL/mol [Silva et al, 19861) or yeast enolase (60 mL/mol [Paladini & Weber, 1981bl). Previous studies indicate that electrostriction decreases the volume of a system (Heremans, 1982;Weber & Drickamer, 1983). This would suggest that a binding process involving a calcium bridge between two anionic components, as proposed for vitamin K-dependent proteins with membranes, would be reversed as pressure is increased because of the negative change in volume due to electrostriction.…”

“…The primary contributors to volume changes are void volumes, which result from the imperfect interfacing of two macromolecular surfaces; electrostriction, the tighter packing of water molecules around an exposed charge (Heremans, 1982;Weber & Drickamer, 1983); exchange of more tightly packed polar (solvation) for nonpolar interactions; and lipid condensation in cases involving a membrane (Ceuterick et al, 1979;Deckmann et al, 1985;Wong, 1987). Aromatic ring interactions are associated with negative A Vs and are strengthened by increased pressure (Harrington & Kegeles, 1973;Heremans, 1982;Weber, 1987;Dannenberg et al, 1990).…”

“…Aromatic ring interactions are associated with negative A Vs and are strengthened by increased pressure (Harrington & Kegeles, 1973;Heremans, 1982;Weber, 1987;Dannenberg et al, 1990). Changes in protein tertiary structure typically are not observed at pressures less than 2.5 kbar (Heremans, 1982;Weber & Drickamer, 1983). Thus, high pressure can be a useful tool for identifying the type of forces involved in macromolecular interactions.…”