Identification of in vivo substrates of the chaperonin GroEL
Article Abstract:
It has been possible to identify a large number of the endogenous substrates of the chaperonin GroEL. Many of these substrates are structurally labile and interact with GroEL both for the initial folding and for conformational maintenance during their lifetime in the cell. Structural analysis has indicated that these proteins have a complex domain architecture, preferentially containing two or more domains with alpha-beta-folds. The typical GroEL substrate was found to have an Mr of between 20K and 60K.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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A TCP1-related molecular chaperone from plants refolds phytochrome to its photoreversible form
Article Abstract:
A new protein appears to be the cytosolic chaperone responsible for phytochrome biogenesis in plant cells. The protein is related to t-complex polypeptide-1, or TCP1, which mediates cytoskeletal folding in mammalian cells. The new protein was copurified with the photoreceptor from etiolated oat seedlings. Its size and configuration are distinct, with two stacked rings of six subunits each.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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A quantum revolution
Article Abstract:
A final spectacular proof for superfluidity frictionless flow in an ultracold gas of fermionic atoms is presented. The size of the fermion pairs is small compared with the typical interparticle distances, which ultimately result in the formation of a closely bound, bosonic molecule.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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