Results 191 to 200 of about 30,272 (208)

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
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GroEL and the GroEL-GroES Complex

2017
Chaperonin is categorized as a molecular chaperone and mediates the formation of the native conformation of proteins by first preventing folding during synthesis or membrane translocation and subsequently by mediating the step-wise ATP-dependent release that result in proper folding.
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Structural aspects of GroEl function

Current Opinion in Structural Biology, 1998
The chaperonin GroEL and its cofactor GroES facilitate protein folding in an ATP-regulated manner. The recently solved crystal structure of the GroEL.GroES.(ADP)7 complex shows that the lining of the cavity in the polypeptide acceptor state is hydrophobic, whereas in the protein-release state it becomes hydrophilic.
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From Minichaperone to GroEL 3: Properties of an Active Single-ring Mutant of GroEL

Journal of Molecular Biology, 2000
The next step in our reductional analysis of GroEL was to study the activity of an isolated single seven-membered ring of the 14-mer. A known single-ring mutant, GroEL(SR1), contains four point mutations that prevent the formation of double-rings. That heptameric complex is functionally inactive because it is unable to release GroES.
J, Chatellier, F, Hill, N W, Foster, P, Goloubinoff, A R, Fersht   +4 more
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From Minichaperone to GroEL 1: Information on GroEL-Polypeptide Interactions from Crystal Packing of Minichaperones†

Journal of Molecular Biology, 2000
We are reconstructing the mechanism of action of GroEL by a reductionist approach of isolating its minimal fragment that has residual activity (the "minichaperone" core) and then identifying how additional elements of structure confer further activity and function. We report here the 2.0 A resolution crystal structure of the minichaperone GroEL(193-345)
Q, Wang, A M, Buckle, A R, Fersht
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?????????????????? ?????????????????????????????? ???????????????? GroEL ?? ?????? ???????????????????????????????? ??????????-???????????????????????? ?? Hsp60

2019
The method of obtaining and purification of recombinant chaperon GroEL (prokaryotic homolog of eukaryotic chaperon Hsp60) including the protein expression in E. coli cells, precipitation with saturated ammonium sulphate from a producent lysate, gel-filtration on Sephacryl-300 column and ion-exchange chromatography on MonoQ HR 5/5 column, is described ...
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Nature and Consequences of GroEL-Protein Interactions

Biochemistry, 1995
The importance of chaperonin-protein interactions has been investigated by analyzing the refolding of the barley chymotrypsin inhibitor 2 in the presence of GroEL. The chaperonin retards the rate of refolding of wild type and 32 representative point mutants.
Itzhaki, Laura S., Otzen, Daniel E., Fersht, Alan R.   +2 more
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Structure and Allostery of the Chaperonin GroEL

Journal of Molecular Biology, 2013
Chaperonins are intricate allosteric machines formed of two back-to-back, stacked rings of subunits presenting end cavities lined with hydrophobic binding sites for nonnative polypeptides. Once bound, substrates are subjected to forceful, concerted movements that result in their ejection from the binding surface and simultaneous encapsulation inside a ...
Helen R, Saibil, Wayne A, Fenton, Daniel K, Clare, Arthur L, Horwich   +3 more
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Residual Structure in Urea-Denatured Chaperonin GroEL

Biochemistry, 1995
The urea denaturation of the chaperonin GroEL has been studied by circular dichroism, intrinsic tyrosine fluorescence and fluorescence of the hydrophobic probe, 1,1'-bis(4-anilino)naphthalene-5,5'-disulfonic acid (bisANS). It is shown that GroEL denaturation, monitored by CD and intrinsic fluorescence measurements, can be well described by a two-state ...
B M, Gorovits, J W, Seale, P M, Horowitz
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Oxidized GroEL can function as a chaperonin

Frontiers in Bioscience, 2004
Here, we report on the facilitated reactivation (85%) of oxidatively inactivated rhodanese by an oxidized form of the molecular chaperone GroEL (ox-GroEL). Reactivation by ox-GroEL required a reductant, and the enzyme substrate, sodium thiosulfate.
Girish C, Melkani, Gustavo, Zardeneta, Jose A, Mendoza   +2 more
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