Results 41 to 50 of about 8,357 (212)
Friends in need: How chaperonins recognize and remodel proteins that require folding assistance
Frontiers in Molecular Biosciences, 2022 Chaperonins are biological nanomachines that help newly translated proteins to fold by rescuing them from kinetically trapped misfolded states. Protein folding assistance by the chaperonin machinery is obligatory in vivo for a subset of proteins in the ...
George Stan +3 more
doaj +1 more source
Streptomyces lividans groES, groEL1 and groEL2 genes [PDF]
Microbiology, 1997 The Streptomyces lividans groES/ELI operon and groEL2 gene were cloned and their respective DNA sequences determined. The sequenced DNA comprised the genes and their respective regulatory regions in both cases. Transcription of both groES/EL1 and groEL2 seemed to be subjected to temporal control at 30 °C.
Patricia, de León +5 more
openaire +2 more sources
Proteins: Structure, Function, and Bioinformatics, EarlyView.ABSTRACT Proteins are built from modular domains that serve as fundamental units of structure and evolution. While individual domains have been extensively cataloged, their collective distribution across the lineages of life has remained poorly resolved.
Rui Guo +5 more
wiley +1 more source
Proteome-Wide Analyis of Chaperonin-Dependent Protein Folding in Escherichia coli [PDF]
, 2006 In Escherichia coli, the cylindrical chaperonin GroEL and its cofactor GroES promote the folding of a fraction of newly synthesized polypeptide chains by acting as an Anfinsen cage.
Maier, T., Maier, Tobias
core
Biotechnology for Biofuels and Bioproducts, 2022 Background Lipoxygenase (EC. 1.13.11.12, LOX) can catalyze the addition of oxygen into polyunsaturated fatty acids to produce hydroperoxides, which are widely used in the food, chemical, and pharmaceutical industries.
Cuiping Pang +5 more
doaj +1 more source
Limits of Protein Folding Inside GroE Complexes [PDF]
Journal of Biological Chemistry, 2000 The GroE chaperones of Escherichia coli promote the folding of other proteins under conditions where no spontaneous folding occurs. One requirement for this reaction is the trapping of the nonnative protein inside the chaperone complex. Encapsulation may be important to prevent unfavorable intermolecular interactions during folding.
H, Grallert, K, Rutkat, J, Buchner
openaire +2 more sources
Russian wheat aphid: a model for genomic plasticity and a challenge to breeders
Insect Science, EarlyView.Invasive foundress finds suitable habitat and reproduces through pathogenesis. Wingless females produce life offspring quickly, which leads to high population densities. High population densities result in competition, which may induce epigenetic changes and wing development for dispersal.
Astrid Jankielsohn +8 more
wiley +1 more source
Characterization of multifunctional proteins from Helicobacter pylori [PDF]
, 2010 This thesis reports the cloning, overexpression and characterization of two interesting proteins from Helicobacter pylori: Heat Shock protein A (HspA), and CoaX (Type III Pantothenate kinase).
Scannella, Alessandra
core
Identifying mHsp60 mutants that are functional with GroES. [PDF]
, 2012 (A) Examination of the in vivo system at the indicated growth conditions. (B) Ten-fold-serial dilutions of E. coli strain MGM100 harboring plasmid pOFX with the indicated mHsp60 variant and GroES, grown on agar plates in the presence of glucose and IPTG.
Galit Levy-Rimler (115146) +8 more
core +1 more source
Biotechnology & Biotechnological Equipment, 2018 Use of thermotolerant strains offers the advantage of conducting production process at elevated temperatures, thereby improving the catalytic efficiency and reducing the energy consumption and the production costs.
Zixing Dong +7 more
doaj +1 more source