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Influence of pressure on protein conformation
Author(s) -
Lüdemann H.D.
Publication year - 1988
Publication title -
makromolekulare chemie. macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 0258-0322
DOI - 10.1002/masy.19880170105
Subject(s) - monomer , chemistry , denaturation (fissile materials) , aqueous solution , biophysics , volume (thermodynamics) , protein structure , thermodynamics , polymer , organic chemistry , biochemistry , biology , nuclear chemistry , physics
The pressure effects in aqueous solutions of biopolymers are presented. It is shown, that pressure in the range of 300 to 800 MPa leads for small monomeric proteins to irreversible denaturation. Larger oligomeric enzymes and structural proteins dissociate reversibly in the pressure range around 100 MPa. The sign of the volume effects of the various noncovalent interactions contributing to the observed reaction and activation volumes is discussed.