Results 171 to 180 of about 8,357 (212)
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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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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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High resolution surface structure ofE. coliGroES oligomer by atomic force microscopy [PDF]
FEBS Letters, 1996 Using atomic force microscopy (AFM) in aqueous solution, we show that the surface structure of the oligomeric GroES can be obtained up to 10 Å resolution. The seven subunits of the heptamer were well resolved without image averaging.
Jianxun Mou +2 more
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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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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
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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 reaction cycle of GroEL and GroES in chaperonin-assisted protein folding [PDF]
Nature, 1993 The reaction mechanism of protein folding by the chaperonin GroEL and its regulator GroES has been defined. GroES and substrate protein counteract each other's effects on GroEL: whereas GroES stabilizes GroEL in the ADP-bound state, binding of unfolded ...
Jörg Martin +2 more
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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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The GroES antigens of Mycobacterium avium and Mycobacterium paratuberculosis
Veterinary Microbiology, 1999The GroES antigen provokes a strong immune response in human beings with tuberculosis or leprosy. We cloned and sequenced the Mycobacterium avium and Mycobacterium paratuberculosis GroES genes. M. avium and M. paratuberculosis have identical GroES sequences which differ from other mycobacterial species. This supports the current formal designation of M.
Richard Frothingham, R Frothingham
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Reversible Oligomerization and Denaturation of the Chaperonin GroES
Biochemistry, 1996The 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 +3 more
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