Solubilization and refolding of bacterial inclusion body proteins
about
Architecture and active site of particulate methane monooxygenaseDevelopments in purification methods for obtaining and evaluation of collagen derived endogenous angioinhibitorsThe Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-xEvolutionary patterning: a novel approach to the identification of potential drug target sites in Plasmodium falciparumStabilizing additives added during cell lysis aid in the solubilization of recombinant proteinsScalable Production of Recombinant Membrane Active Peptides and Its Potential as a Complementary Adjunct to Conventional ChemotherapeuticsAn influenza A/H1N1/2009 hemagglutinin vaccine produced in Escherichia coliThe prediction and characterization of YshA, an unknown outer-membrane protein from Salmonella typhimurium.Characterization of neuronal Src kinase purified from a bacterial expression system.Refolding and purification of recombinant L-asparaginase from inclusion bodies of E. coli into active tetrameric protein.Effect of charged amino acid side chain length on lateral cross-strand interactions between carboxylate- and guanidinium-containing residues in a β-hairpin.Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process.A baseline process for the production, recovery, and purification of bacterial influenza vaccine candidates.Rotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences.Construction of a series of vectors for high throughput cloning and expression screening of membrane proteins from Mycobacterium tuberculosis.Synthesis and analysis of separation networks for the recovery of intracellular chemicals generated from microbial-based conversions.Controlled localization of functionally active proteins to inclusion bodies using leucine zippersAn approach to the production of soluble protein from a fungal gene encoding an aggregation-prone xylanase in Escherichia coli.Kinetic and structural characterization of human mortalinHighly efficient production of soluble proteins from insoluble inclusion bodies by a two-step-denaturing and refolding methodKinetics of inclusion body formation and its correlation with the characteristics of protein aggregates in Escherichia coli.Complete solubilization and purification of recombinant human growth hormone produced in Escherichia coli.Overproduction and biophysical characterization of human HSP70 proteins.Towards revealing the structure of bacterial inclusion bodies.Comparison of two codon optimization strategies to enhance recombinant protein production in Escherichia coli.A novel hyaluronidase from brown spider (Loxosceles intermedia) venom (Dietrich's Hyaluronidase): from cloning to functional characterization.Refolding by high pressure of a toxin containing seven disulfide bonds: bothropstoxin-1 from Bothrops jararacussuUsing electrospray laser desorption ionization mass spectrometry to rapidly examine the integrity of proteins stored in various solutions.A single freeze-thawing cycle for highly efficient solubilization of inclusion body proteins and its refolding into bioactive formOne-step refolding and purification of recombinant human tumor necrosis factor-α (rhTNF-α) using ion-exchange chromatography.Overview of the purification of recombinant proteins.Characterization of the 4,6-α-glucanotransferase GTFB enzyme of Lactobacillus reuteri 121 isolated from inclusion bodies.Expression of a codon-optimised recombinant Ara h 2.02 peanut allergen in Escherichia coli.Increased yield of high purity recombinant human interferon-gamma utilizing reversed phase column chromatographyDesign, purification and assessment of GRP78 binding peptide-linked Subunit A of Subtilase cytotoxic for targeting cancer cells.The Optimization of Soluble PTEN Expression in Escherichia coliSoluble Expression and Characterization of Biologically Active Bacillus anthracis Protective Antigen in Escherichia coli.One-step affinity tag purification of full-length recombinant human AP-1 complexes from bacterial inclusion bodies using a polycistronic expression system.Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry.Purification of proteins fused to glutathione S-transferase.
P2860
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P2860
Solubilization and refolding of bacterial inclusion body proteins
description
2005 nî lūn-bûn
@nan
2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Solubilization and refolding of bacterial inclusion body proteins
@ast
Solubilization and refolding of bacterial inclusion body proteins
@en
Solubilization and refolding of bacterial inclusion body proteins
@nl
type
label
Solubilization and refolding of bacterial inclusion body proteins
@ast
Solubilization and refolding of bacterial inclusion body proteins
@en
Solubilization and refolding of bacterial inclusion body proteins
@nl
prefLabel
Solubilization and refolding of bacterial inclusion body proteins
@ast
Solubilization and refolding of bacterial inclusion body proteins
@en
Solubilization and refolding of bacterial inclusion body proteins
@nl
P3181
P356
P1476
Solubilization and refolding of bacterial inclusion body proteins
@en
P2093
Amulya Kumar Panda
Surinder Mohan Singh
P304
P3181
P356
10.1263/JBB.99.303
P407
P577
2005-04-01T00:00:00Z