-
folding of many proteins. To
function properly,
GroEL requires the lid-like
cochaperonin protein complex GroES. In
eukaryotes the
organellar proteins Hsp60...
- mitochondria. The
GroEL/
GroES
complex in E. coli is a
Group I
chaperonin and the best
characterized large (~ 1 MDa)
chaperonin complex.
GroEL is a double-ring...
- 54-kDa GFP in its lumen.
GroES (Hsp10) is a single-ring
heptamer that
binds to
GroEL in the
presence of ATP or ADP.
GroEL/
GroES may not be able to undo...
- HSPE1 gene. The
homolog in E. coli is
GroES that is a
chaperonin which usually works in
conjunction with
GroEL.
GroES
exists as a ring-shaped
oligomer of...
-
uniquely identified by a few
conserved signature indel (CSI) in the HSP60 (
GroEL) protein. In addition, a
number of
bacterial taxa (including Negativicutes...
-
nature of the Hsp90
knockdown used in that experiment. The
overproduction of
GroEL in
Escherichia coli
increases mutational robustness. This can
increase evolvability...
-
conserved signature indels in a
number of
important proteins (viz. DnaK,
GroEL). Of
these two
structurally distinct groups of bacteria,
monoderms are indicated...
-
GroEL homolog, a
molecular chaperon essential for
protein folding. Therefore,
after feeding B.
tabaci with a diet
containing antiserum against GroEL,...
- state,
characterisation of
complex macromolecular ****emblies (ribosomes,
GroEL, AAV) and
protein interactions such as protein-protein interactions. M****...
-
proteins in an ATP-dependent manner.
Examples of
foldase systems are the
GroEL/
GroES and the DnaK/DnaJ/GrpE system. Hoffmann, J. R. H.; Linke, K.; Graf,...
