Clitocypin, a new cysteine proteinase inhibitor, is monomeric: impact on the mechanism of folding.
The molecular mass of clitocypin, a new type of cysteine proteinase inhibitor from the mushroom Clitocybe nebularis, has been determined by analytical ultracentrifugation and gel exclusion chromatography. The result is in agreement with the formula mass of 16.8 kDa, demonstrating that the inhibitor is a monomer in aqueous solution. This enables the kinetics of unfolding and refolding to be interpreted in terms of folding in a kinetically two state, highly cooperative transition from the thermally unfolded state.
Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Jamova, 39, 1000 Ljubljana, Slovenia.
Katja
K
Galesa
Richard M
RM
Thomas
Marjetka
M
Kidric
Roger H
RH
Pain
D002850:Chromatography, Gel; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology*; D019281:Dimerization; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005656:Fungal Proteins / Q000737:chemistry / Q000502:physiology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D013696:Temperature; D013997:Time Factors; D014461:Ultracentrifugation
C411656:Clitocypin protein, Clitocybe nebularis; D015853:Cysteine Proteinase Inhibitors; D004791:Enzyme Inhibitors; D005656:Fungal Proteins