NASA Logo

NTRS

NTRS - NASA Technical Reports Server

Back to Results
Localization of the chaperone binding siteThe hypothesis derived from models of the multi-oligomeric chaperone complex suggests that partially denatured proteins bind in a central cavity in the aggregate. To test this hypothesis, the molecular chaperone, alpha crystallin, was bound to partially denatured forms of gamma crystallin, and the binding site was visualized by immunogold localization. In an alternative approach, gold particles were directly complexed with gamma crystallin, followed by binding to the alpha crystallin aggregate. In both cases, binding was localized to the central region of the aggregate, confirming for the first time that partially denatured proteins do indeed bind to a central region of the molecular chaperone aggregate.
Document ID
20050000468
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
External Source(s)
Authors
Boyle, D.
(Kansas State University Manhattan 66506)
Gopalakrishnan, S.
Takemoto, L.
Spooner, B. S.
Date Acquired
August 22, 2013
Publication Date
May 14, 1993
Publication Information
Publication: Biochemical and biophysical research communications
Volume: 192
Issue: 3
ISSN: 0006-291X
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
Non-NASA Center
NASA Discipline Cell Biology

Available Downloads

There are no available downloads for this record.
No Preview Available