Results 141 to 150 of about 9,153 (190)
GroES and the chaperonin-assisted protein folding cycle: GroES has no affinity for nucleotides [PDF]
FEBS Letters, 1995 The E. coli chaperonin proteins, GroEL and GroES, assist in folding newly synthesized proteins. GroES is necessary for GroEL‐assisted folding under conditions where the substrate protein cannot spontaneously fold. On the basis of photolabelling of GroES with 8‐azido‐ATP, a role for nucleotide binding to GroES in chaperonin function was suggested ...
Ernesto Freire +2 more
exaly +5 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.
Olga Boudker, Ernesto Freire
exaly +3 more sources
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GroES Promotes the T to R Transition of the GroEL Ring Distal to GroES in the GroEL−GroES Complex†
Biochemistry, 1997Curves 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
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A biochemical screen for GroEL/GroES inhibitors
Bioorganic and Medicinal Chemistry Letters, 2014High-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 +2 more
exaly +3 more sources
Lord of the Rings: GroES Structure
Science, 1996The 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
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Refolding of Barnase in the Presence of GroE
Journal of Molecular Biology, 1993The 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
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Evidence for GroES Acting as a Transcriptional Regulator
Biochemical and Biophysical Research Communications, 1996Cochaperonins (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 +6 more
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Nature Structural Biology, 1996
The stuctures of the co-chaperonin GroES and of the GroEL•ATPγS complex raise a host of tantalizing questions and whet the appetite for even more challenging structures, the various GroEL•nucleotide•GroES complexes which facilitate folding.
George H. Lorimer, Matthew J. Todd
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The stuctures of the co-chaperonin GroES and of the GroEL•ATPγS complex raise a host of tantalizing questions and whet the appetite for even more challenging structures, the various GroEL•nucleotide•GroES complexes which facilitate folding.
George H. Lorimer, Matthew J. Todd
openaire +1 more source
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
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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
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THE UNIVERSALLY CONSERVED GroE (Hsp60) CHAPERONINS
Annual Review of Microbiology, 1991INTRODUCTION . . . . . . . . . . . . . . . . . . . . . . .. . . . . . . . . .. . . .. . . .. . . . . ... ...... . . . . . . . . . . . . . . . . ... . . . . . . . . . . 301 THE groE OPERON . . . . . . . . . . . .... . . . . . . . . . . . . . . . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
J, Zeilstra-Ryalls +2 more
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