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Symmetric complexes of GroE chaperonins as part of the functional cycle.

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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Abstract

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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Item Type:Article
Date:1994
Institutions:UNSPECIFIED
Identification Number:
ValueType
7913554PubMed ID
Classification:
NotationType
Adenosine Diphosphate/pharmacologyMESH
Adenosine Triphosphatases/metabolismMESH
Adenosine Triphosphate/metabolismMESH
Bacterial Proteins/ultrastructureMESH
BiopolymersMESH
Chaperonin 10MESH
Chaperonin 60MESH
Heat-Shock Proteins/ultrastructureMESH
HydrolysisMESH
Microscopy, ElectronMESH
Protein BindingMESH
Subjects:UNSPECIFIED
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:08 Mar 2010 06:56
Last Modified:08 Mar 2010 06:56
Item ID:13267
Owner Only: item control page
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