Results 181 to 190 of about 18,538 (219)

Groel crystal growth and characterization

Biosystems, 2008
Single crystals of ribosomal proteins obtained for the first time by Langmuir-Blodgett (LB) nanotemplate confirm earlier findings (Pechkova et al., 2008), pointing to a new generation of bionanomaterials of unique structure-function relationship. The ribosomal protein phage GroEL was overexpressed in E. coli.
PESHKOVA, EVGENIYA, TRIPATHI S, SPERA, ROSANNA, NICOLINI, CLAUDIO   +3 more
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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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Purification and Handling of the Chaperonin GroEL

2021
GroEL is an important model molecular chaperone. Despite being extensively studied, several critical aspects of its functionality are still in dispute due partly to difficulties in obtaining protein samples of consistent purity. Here I describe an easy-to-carry-out purification protocol that can reliably produce highly purified and fully functional ...
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Insertion mutagenesis of Escherichiacoli GroEL

Biochemical and Biophysical Research Communications, 2003
To gain insights into the in vivo folding and assembly of bacterial chaperonins, groEL was subjected to insertion mutagenesis using transposon ISlacZ/in. Four GroEL-LacZ fusions and the corresponding insertion mutants were obtained after residues 34, 90, 291, and 367. Apical domain insertion mutants GroEL291 and GroEL367 were degraded into monomeric 30-
Danielle, Amatore, François, Baneyx
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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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Crystal Structure of Wild-type Chaperonin GroEL [PDF]

Journal of Molecular Biology, 2005
The 2.9A resolution crystal structure of apo wild-type GroEL was determined for the first time and represents the reference structure, facilitating the study of structural and functional differences observed in GroEL variants.
Doriano Lamba, Saulius Grazulis, Hermann Heumann   +2 more
exaly   +2 more sources

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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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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?????????????????? ?????????????????????????????? ???????????????? 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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