• Thumbnail for GroEL
    folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex GroES. In eukaryotes the organellar proteins Hsp60...
    42 KB (5,438 words) - 11:57, 16 January 2024
  • Thumbnail for Chaperonin
    mitochondria. The GroEL/GroES complex in E. coli is a Group I chaperonin and the best characterized large (~ 1 MDa) chaperonin complex. GroEL is a double-ring...
    21 KB (2,312 words) - 11:30, 25 November 2023
  • Thumbnail for Chaperone (protein)
    54-kDa GFP in its lumen. GroES (Hsp10) is a single-ring heptamer that binds to GroEL in the presence of ATP or ADP. GroEL/GroES may not be able to undo...
    29 KB (3,499 words) - 07:16, 20 February 2024
  • Thumbnail for GroES
    HSPE1 gene. The homolog in E. coli is GroES that is a chaperonin which usually works in conjunction with GroEL. GroES exists as a ring-shaped oligomer of...
    34 KB (4,104 words) - 21:30, 11 April 2024
  • Thumbnail for Gram-positive bacteria
    conserved signature indels in a number of important proteins (viz. DnaK, GroEL). Of these two structurally distinct groups of bacteria, monoderms are indicated...
    24 KB (2,655 words) - 23:06, 30 May 2024
  • GroEL homolog, a molecular chaperon essential for protein folding. Therefore, after feeding B. tabaci with a diet containing antiserum against GroEL,...
    10 KB (1,363 words) - 18:48, 6 December 2023
  • Thumbnail for Gram-negative bacteria
    uniquely identified by a few conserved signature indel (CSI) in the HSP60 (GroEL) protein. In addition, a number of bacterial taxa (including Negativicutes...
    24 KB (2,444 words) - 16:21, 29 May 2024
  • nature of the Hsp90 knockdown used in that experiment. The overproduction of GroEL in Escherichia coli increases mutational robustness. This can increase evolvability...
    21 KB (2,607 words) - 03:59, 17 April 2024
  • proteins in an ATP-dependent manner. Examples of foldase systems are the GroEL/GroES and the DnaK/DnaJ/GrpE system. Holdase Chaperonin Co-chaperone Hoffmann...
    933 bytes (80 words) - 03:22, 12 May 2024
  • Thumbnail for Dihydrofolate reductase
    Hartl FU (February 1996). "Protein folding in the central cavity of the GroEL-GroES chaperonin complex". Nature. 379 (6564): 420–6. Bibcode:1996Natur.379...
    40 KB (4,581 words) - 23:34, 26 January 2024
  • Thumbnail for Coxiellaceae
    Subject Headings (MeSH) Leclerque A, Kleespies RG (April 2008). "16S rRNA-, GroEL- and MucZ-based assessment of the taxonomic position of 'Rickettsiella melolonthae'...
    1 KB (105 words) - 09:14, 18 March 2022
  • AL (Nov 17, 1995). "Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES". Cell. 83 (4): 577–87. doi:10...
    6 KB (400 words) - 18:36, 5 January 2024
  • state, characterisation of complex macromolecular assemblies (ribosomes, GroEL, AAV) and protein interactions such as protein-protein interactions. Mass...
    12 KB (1,471 words) - 00:31, 21 May 2024
  • unequivocally unfolded protein and the purified chaperonin proteins GroEL and GroES, his group was the first to demonstrate the ATP-dependent folding...
    5 KB (419 words) - 13:58, 15 August 2023
  • Thumbnail for Protein tertiary structure
    function and may assist most globular proteins, for example, the prokaryotic GroEL/GroES system of proteins and the homologous eukaryotic heat shock proteins...
    15 KB (1,603 words) - 17:26, 23 April 2024
  • Thumbnail for Protein folding
    particles during infection. Like GroES, gp31 forms a stable complex with GroEL chaperonin that is absolutely necessary for the folding and assembly in...
    76 KB (8,677 words) - 00:23, 28 May 2024
  • structure which further increases its heat resistance. Overexpression of GroES and GroEL chaperones that help the correct folding of proteins in situations...
    15 KB (1,867 words) - 13:14, 9 January 2024
  • Heat shock proteins/ Chaperonins Hsp10/GroES Hsp27 Hsp47 HSP60/GroEL Hsp40/DnaJ A1 A2 A3 B1 B2 B11 B4 B6 B9 C1 C3 C5 C6 C7 C10 C11 C13 C14 C19 Hsp70 1A...
    49 KB (5,525 words) - 05:03, 26 April 2024
  • Thumbnail for Cryogenic electron microscopy
    determine protein structure from monodisperse samples. Cryo-EM image of GroEL suspended in amorphous ice at 50000× magnification Structure of alcohol...
    23 KB (2,514 words) - 07:30, 10 May 2024
  • signature indels in a number of important proteins (for example, DnaK and GroEL). As shown in the figure to the right, the periplasmic space in gram-negative...
    20 KB (2,287 words) - 03:21, 23 March 2024
  • Thumbnail for Orientia tsutsugamushi
    which are very similar to GroES and GroEL of the bacterium Escherichia coli, but not that of Rickettsia species. GroES and GroEL are heat shock proteins...
    66 KB (8,133 words) - 20:27, 17 May 2024
  • Thumbnail for TRiC (complex)
    multiprotein complex and the chaperonin of eukaryotic cells. Like the bacterial GroEL, the TRiC complex aids in the folding of ~10% of the proteome, and actin...
    6 KB (433 words) - 23:28, 15 November 2022
  • Thumbnail for Capsid
    GroES and able to substitute for it in the assembly of bacteriophage T4 virions during infection. Like GroES, gp31 forms a stable complex with GroEL chaperonin...
    22 KB (2,554 words) - 01:23, 21 April 2024
  • Duodecimal (redirect from El (number))
    100 is "gro"; BA9 is "el gro dek do nine"; B86 is "el gro eight do six"; 8BB,15A is "eight gro el do el, one gro five do dek"; ABA is "dek gro el do dek";...
    64 KB (4,455 words) - 14:25, 15 May 2024
  • 1038/nature06384. PMID 18046402. S2CID 2497138. Käll L, Krogh A, Sonnhammer EL (May 2004). "A combined transmembrane topology and signal peptide prediction...
    15 KB (1,741 words) - 18:05, 31 December 2023
  • coli counterpart of the eukaryotic HSP60 protein, known as GroEL, and its helper protein GroES. His group showed chaperone-mediated folding actually consisted...
    35 KB (2,564 words) - 10:46, 3 February 2024
  • RNA polymerase II holoenzyme, symmetric viral capsids, complex of GroEL and GroES; membrane protein complexes: porosome, photosystem I, ATP synthase...
    28 KB (2,348 words) - 03:23, 19 February 2024
  • Thumbnail for Protein contact map
    ; Horovitz, A. (2002). "Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations". Proteins. 48 (4): 611–617. doi:10...
    16 KB (1,979 words) - 15:06, 8 September 2023
  • been possible to study proteins in complex with the 900 kDa chaperone GroES-GroEL. Structure determination by NMR has traditionally been a time-consuming...
    43 KB (5,327 words) - 02:04, 20 September 2023
  • of low copy number plasmids The co-expression of chaperone (such as GroES-GroEL and DnaK-DnaJ-GrpE) The use of specific E. coli strains such as (AD494...
    23 KB (2,550 words) - 08:34, 27 April 2024