Abstract:
:The effect of hydrostatic pressure upon solutions of chymotrypsinogen and lysozyme at room temperature has been followed by employing a new technique [Chryssomallis, G. S., Drickamer, H. G., & Weber, G. (1978) J. Appl. Phys. 49, 3084] that permits the measurement of fluorescence polarization at pressures of up to 10 kbar. Lysozyme shows a stable, reversible 60% increase in apparent volume when the pressure is raised to 9 kbar. This can be given a simple interpretation in terms of solvent penetration of the structure at higher pressures. In contrast, the results with chymotrypsinogen are time dependent and only partially reversible on release of the pressure. They involve conversion (tl/e = 5 min) to a form with a lower rotational rate at approximately 6 kbar and return to a fast-rotating form at higher pressure. This latter form persists on pressure release. The possibility of generating what are clearly metastable conformations, not only in chymotrypsinogen but also in flavodoxins [Visser, A. J. W. G., Li, T. M., Drickamer, H. G., & Weber, G. (1977) Biochemistry 16, 4879], indicates that there are unresolved questions about the relative stability of protein conformations which can be profitably investigated by high-pressure experiments.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Chryssomallis GS,Torgerson PM,Drickamer HG,Weber Gdoi
10.1021/bi00517a002subject
Has Abstractpub_date
1981-07-07 00:00:00pages
3955-9issue
14eissn
0006-2960issn
1520-4995journal_volume
20pub_type
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