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Recombinant homo- and hetero-oligomers of an ultrastable chaperonin from the archaeon Pyrodictium occultum show chaperone activity in vitro.

Minuth, T. and Frey, G. and Lindner, P. and Rachel, Reinhard and Stetter, Karl Otto and Jaenicke, R. (1998) Recombinant homo- and hetero-oligomers of an ultrastable chaperonin from the archaeon Pyrodictium occultum show chaperone activity in vitro. European journal of biochemistry / FEBS 258 (2), pp. 837-845.

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Abstract

The archaeon Pyrodictium occultum is one of the most thermophilic organisms presently known. Previous experiments provided support for the significant contribution of a high-molecular-mass protein complex to the extreme thermotolerance of P. occultum. This protein complex, the 'thermosome', is composed of two subunits, alpha and beta, which form a hexadecameric double ring complex. In order to ...

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Item Type:Article
Date:1998
Institutions:Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie > Prof. Dr. Michael Thomm
Identification Number:
ValueType
9874254PubMed ID
Classification:
NotationType
Adenosine Triphosphatases/metabolismMESH
Archaeal Proteins/ultrastructureMESH
Chaperonins/ultrastructureMESH
Circular DichroismMESH
Desulfurococcaceae/chemistryMESH
Electrophoresis, Polyacrylamide GelMESH
Enzyme StabilityMESH
KineticsMESH
Microscopy, ElectronMESH
Molecular Sequence DataMESH
Protein ConformationMESH
Recombinant Proteins/ultrastructureMESH
Scattering, RadiationMESH
TemperatureMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Owner: Gertraud Kellers
Deposited On:03 Mar 2010 07:53
Last Modified:03 Mar 2010 07:53
Item ID:13177
Owner Only: item control page
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