Results 161 to 170 of about 8,317 (219)

Molecular, structural, and functional characterization of delta subunit of T-complex protein-1 from <i>Leishmania donovani</i>. [PDF]

Infect Immun
Anand A, Gautam G, Srivastava G, Yadav S, Ramalingam K, Siddiqi MI, Goyal N.   +6 more
europepmc   +1 more source

Recombinant Production of a TRAF-Domain Lectin from Cauliflower: A Soluble Expression Strategy for Functional Protein Recovery in <i>E. coli</i>. [PDF]

Int J Mol Sci
Ludgero AKM, da Silva ALA, Cruz LH, Brazão CAC, Taylor KMH, de Oliveira LL, Bragança CRS, Duarte CEM.   +7 more
europepmc   +1 more source

Understanding carboxysomes to enhance carbon fixation in crops. [PDF]

Biochem Soc Trans
Nguyen ND, Rourke LM, Cleaver A, Brock J, Long BM, Price DG.   +5 more
europepmc   +1 more source

External Force Field for Protein Folding in ChaperoninsPotential Application in In Silico Protein Folding

ACS Omega
Irena Roterman, Katarzyna Stapor, Dawid Dułak, Leszek Konieczny   +3 more
doaj   +1 more source

The structural basis of eukaryotic chaperonin TRiC/CCT: Action and folding. [PDF]

Mol Cells
Kim H, Park J, Roh SH.
europepmc   +1 more source

Molecular Chaperonin HSP60: Current Understanding and Future Prospects. [PDF]

Int J Mol Sci
Singh MK, Shin Y, Han S, Ha J, Tiwari PK, Kim SS, Kang I.   +6 more
europepmc   +1 more source

Origin of chaperone dependence and assembly complexity in Rubisco’s biogenesis

Ng JZY, Wiens D, Schulz L, Hergenröder A, Küffner AM, Geil C, Erb TJ, Hochberg GKA.   +7 more
europepmc   +1 more source

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Purification of chaperonins

Journal of Chromatography B: Biomedical Sciences and Applications, 1999
The availability of protein samples of sufficient quality and in sufficient quantity is a driving force in biology and biotechnology. Protein samples that are free of critical contaminants are required for specific assays. Large amounts of highly homogeneous and reproducible material are needed for crystallography and nuclear magnetic resonance studies
E, Quaite-Randall, A, Joachimiak
openaire   +2 more sources

Review: Allostery in Chaperonins

Journal of Structural Biology, 2001
Chaperonins mediate protein folding in an ATP-dependent manner. ATP binding and hydrolysis by chaperonins are subject to both homotropic and heterotropic allosteric regulation. In the case of GroEL and CCT, homotropic regulation by ATP is manifested in nested cooperativity, which involves positive intra-ring cooperativity and negative inter-ring ...
Amnon Horovitz
exaly   +3 more sources

Chaperonin: Co-chaperonin Interactions

2014
Co-chaperonins function together with chaperonins to mediate ATP-dependent protein folding in a variety of cellular compartments. Chaperonins are evolutionarily conserved and form two distinct classes, namely, group I and group II chaperonins. GroEL and its co-chaperonin GroES form part of group I and are the archetypal members of this family of ...
openaire   +3 more sources