Source:
Generated By: https://synbiohub.org/public/igem/igem2sbol/1
Created by: Michael James George Milevskiy
Date created: 2009-09-07 11:00:00
Date modified: 2015-05-08 01:11:23
GroEL is a chaperone protein that prevents polypeptide misfolding.
| Types | DnaRegion |
| Roles | CDS Coding |
| Sequences | BBa_K205000_sequence (Version 1) |
Description
GroEL is a chaperone protein that is responsible for the prevention of polypeptide mis-folding. In conjunction with GroES, these two subunits form an assembly dimer that are promote efficient protein folding, especially under stressful conditions such as heat shock. This chaperone protein belongs to the eukaryotic HSP60 (heat shock protein) family.http://www.uniprot.org/uniprot/P0A6F5
Notes
Gene was provided by Christos Kyratsous, we used mutagenesis to remove the internal restriction site, EcoR1, BamH1Source
Christos KyratsousColumbia Univ, Coll Phys & Surg, Dept Microbiol, New York, NY 10032 USA
Ref: Kyratsous, CA, Silverstein, SJ, DeLong, CR, Panagiotidis, CA. (2009) "Chaperone-fusion expression plasmid vectors for improved solubility of recombinant proteins in Escherichia coli" GENE VOL: 440 Issue: 1-2 Pages: 9-15 Date: Jul 1 2009
| Sequence Annotation | Location | Component / Role(s) |
| Start of GroEL End of GroEL Mutation from t to c to remove BamHI restriction site | 1,3 1597,1599 1485,1485 | feature/start start_codon stop_codon feature/stop point_mutation feature/s_mutation |