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Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60

Authors :
Vies, Saskia M. van der
Viitanen, Paul V.
Gatenby, Anthony A.
Lorimer, George H.
Jaenicke, Rainer
Source :
Biochemistry. April 14, 1992, Vol. 31 Issue 14, p3635, 10 p.
Publication Year :
1992

Abstract

Conformational analysis of ribulosebisphosphate carboxylase (Rubisco) from Rhodospirillum rubrum revealed two acid-denatured states and two folded states. The acid-denatured states were comprised of UA1 state, an unfolded and monomeric conformation at pH2 and low ionic strength and A1 state, which was an intermediate conformation at the same pH but at high ionic strength. N1 and N2 states comprised the folded conformational states and were noted be homologous in their secondary state. An unstable fifth conformational state was observed and was found to form a stable binary complex in the presence of chaperonin 60 oligomer.

Details

ISSN :
00062960
Volume :
31
Issue :
14
Database :
Gale General OneFile
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
edsgcl.14261144