Protein aggregation: folding aggregates, inclusion bodies and amyloid
AL Fink - Folding and design, 1998 - cell.com
Aggregation results in the formation of inclusion bodies, amyloid fibrils and folding
aggregates. Substantial data support the hypothesis that partially folded intermediates are …
aggregates. Substantial data support the hypothesis that partially folded intermediates are …
Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins fromE. coli To fold or to refold
JG Thomas, A Ayling, F Baneyx - Applied biochemistry and biotechnology, 1997 - Springer
The high-level expression of recombinant gene products in the gramnegative bacterium
Escherichia coli often results in the misfolding of the protein of interest and its subsequent …
Escherichia coli often results in the misfolding of the protein of interest and its subsequent …
[HTML][HTML] Protein aggregation as bacterial inclusion bodies is reversible
Inclusion bodies are refractile, intracellular protein aggregates usually observed in bacteria
upon targeted gene overexpression. Since their occurrence has a major economical impact …
upon targeted gene overexpression. Since their occurrence has a major economical impact …
Is protein folding a thermodynamically unfavorable, active, energy-dependent process?
The prevailing current view of protein folding is the thermodynamic hypothesis, under which
the native folded conformation of a protein corresponds to the global minimum of Gibbs free …
the native folded conformation of a protein corresponds to the global minimum of Gibbs free …
Membrane protein structural biology: the high throughput challenge
PJ Loll - Journal of structural biology, 2003 - Elsevier
Membrane proteins represent roughly one-third of the proteins encoded in the genome, yet
fewer than 1% of the proteins are of known structure. High-throughput crystallography offers …
fewer than 1% of the proteins are of known structure. High-throughput crystallography offers …
Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: Application of a novel protein folding screen
GQ Chen, E Gouaux - … of the National Academy of Sciences, 1997 - National Acad Sciences
Expression of the S1S2 ligand binding domain [Kuusinen, A., Arvola, M. & Keinänen,
K.(1995) EMBO J. 14, 6327–6332] of the rat α-amino-3-hydroxy-5-methylisoxazole-4 …
K.(1995) EMBO J. 14, 6327–6332] of the rat α-amino-3-hydroxy-5-methylisoxazole-4 …
Understanding the art of producing protein and nonprotein molecules in Escherichia coli
P Balbás - Molecular Biotechnology, 2001 - Springer
The high-level production of functional proteins in E. coli is a very extense field of research
in biotechnology. A number of important aspects to be considered in the initial design of an …
in biotechnology. A number of important aspects to be considered in the initial design of an …
Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease falcipain-2
The Plasmodium falciparum cysteine protease falcipain-2 is a potential new target for
antimalarial chemotherapy. In order to obtain large quantities of active falcipain-2 for …
antimalarial chemotherapy. In order to obtain large quantities of active falcipain-2 for …
Antibody engineering
MS Hayden, LK Gilliland, JA Ledbetter - Current opinion in immunology, 1997 - Elsevier
The development of recombinant techniques for the rapid cloning, expression, and
characterization of cDNAs encoding antibody (Ab) subunits has revolutionized the field of …
characterization of cDNAs encoding antibody (Ab) subunits has revolutionized the field of …
Matrix-assisted refolding of single-chain Fv–cellulose binding domain fusion proteins
We describe a method for the isolation of recombinant single-chain antibodies in a
biologically active form. The single-chain antibodies are fused to a cellulose binding domain …
biologically active form. The single-chain antibodies are fused to a cellulose binding domain …