Results 181 to 190 of about 23,956 (223)

GroES Promotes the T to R Transition of the GroEL Ring Distal to GroES in the GroEL−GroES Complex^†

Biochemistry, 1997
Curves of initial rates of ATP hydrolysis by GroEL as a function of ATP concentration, in the presence of fixed concentrations of GroES, were found to deviate from sigmoidal kinetics. Instead of the lag phase typical of sigmoidal curves, a linear phase is observed at low ATP concentrations.
E, Inbar, A, Horovitz
openaire   +2 more sources

Lord of the Rings: GroES Structure

Science, 1996
The crystal structure of the chaparonin GroES, which together with GroEL assists in the folding of many proteins in Escherichia coli , is reported in this issue of Science by Mande et al . ( p. 203 ). In this Perspective, M. Mayhew and F.
M, Mayhew, F U, Hartl
openaire   +2 more sources

The structural stability of the co-chaperonin GroES

Journal of Molecular Biology, 1997
The structural stability of the co-chaperonin GroES has been studied by high sensitivity differential scanning calorimetry and circular dichroism under different solvent conditions. The thermal folding/unfolding of GroES is a spontaneous reversible process involving a highly cooperative transition between folded heptamers and unfolded monomers.
Ernesto Freire
exaly   +3 more sources

GroEL and GroES

1994
Abstract Both Groel and GroES are essential for growth of E. coli at all temperatures4 Temperature-sensitive, conditional lethal mutants isolated on the basis of blocking phage λgrowth show impaired DNA and RNA synthesis5, a block in cell division that results in formation of long filaments without septa at the non-permissive ...
J Martin, F -U Hartl
openaire   +1 more source

A biochemical screen for GroEL/GroES inhibitors

Bioorganic & Medicinal Chemistry Letters, 2014
High-throughput screening of 700,000 small molecules has identified 235 inhibitors of the GroEL/GroES-mediated refolding cycle. Dose-response analysis of a subset of these hits revealed that 21 compounds are potent inhibitors of GroEL/GroES-mediated refolding (IC50
Steven M, Johnson, Orzala, Sharif, Puiying Annie, Mak, Hsiao-Ting, Wang, Ingo H, Engels, Achim, Brinker, Peter G, Schultz, Arthur L, Horwich, Eli, Chapman   +8 more
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Evidence for GroES Acting as a Transcriptional Regulator

Biochemical and Biophysical Research Communications, 1996
Cochaperonins (cpn10) assist chaperonins (cpn60) in promoting folding and assembly of other proteins. Upon expression of Mycobacterium tuberculosis cpn10 in Escherichia coli we have purified a polypeptide which, through amino acid sequencing, was identified as the endogenous E. coli 10K-S protein.
Legname, Giuseppe, Buono P, Fossati G, Monzini N, Mascagni P, Modena D, Marcucci F.   +6 more
openaire   +2 more sources

NMR analysis of a 900K GroEL–GroES complex

Nature, 2002
Biomacromolecular structures with a relative molecular mass (M(r)) of 50,000 to 100,000 (50K 100K) have been generally considered to be inaccessible to analysis by solution NMR spectroscopy. Here we report spectra recorded from bacterial chaperonin complexes ten times this size limit (up to M(r) 900K) using the techniques of transverse relaxation ...
Arthur L Horwich, Kurt Wüthrich
exaly   +3 more sources

GroE Assists Refolding of Recombinant Human Pro-Urokinase

Journal of Biochemistry, 1997
GroE, one of the molecular chaperones, facilitates correct protein folding both in vitro and in vivo. The refolding of recombinant human pro-urokinase, a protein with a high content of disulfide bonds, was used as a model system to illustrate the mechanism of action of GroE.
Z, Xu, S, Yang, D, Zhu
openaire   +2 more sources

Reversible Oligomerization and Denaturation of the Chaperonin GroES

Biochemistry, 1996
The chaperonin GroEL can assist protein folding and normally acts with the co-chaperonin GroES. These Escherichia coli proteins are encoded on the same operon, with GroES positioned first. In this report, we have investigated the reversible folding of GroES. Using fluorescence anisotropy of dansyl-labeled GroES, intrinsic fluorescence, bis-ANS binding,
J W, Seale, B M, Gorovits, J, Ybarra, P M, Horowitz   +3 more
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Refolding of Barnase in the Presence of GroE

Journal of Molecular Biology, 1993
The refolding of barnase in the presence of GroEL has been monitored on the millisecond to seconds time scale using stopped-flow kinetics. GroEL binds rapidly and tightly to the denatured enzyme with a second-order rate constant of greater than 1.3 x 10(8) s-1 M-1 and slows down greatly the rate of barnase refolding.
T E, Gray, A R, Fersht
openaire   +2 more sources