Schmidt, M. and Rutkat, K. and Rachel, Reinhard and Pfeifer, G. and Jaenicke, R. and Viitanen, P. and Lorimer, G. and Buchner, J. (1994) Symmetric complexes of GroE chaperonins as part of the functional cycle. Science (New York, N.Y.) 265 (5172), pp. 656-659.
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The particular structural arrangement of chaperonins probably contributes to their ability to assist in the folding of proteins. The interaction of the oligomeric bacterial chaperonin GroEL and its cochaperonin, GroES, in the presence of adenosine diphosphate (ADP) forms an asymmetric complex. However, in the presence of adenosine triphosphate (ATP) or its nonhydrolyzable analogs, symmetric ...
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|Created at the University of Regensburg:||Unknown|
|Deposited on:||08 Mar 2010 06:56|
|Last modified:||08 Mar 2010 06:56|