Understanding the relationship between the primary structure of proteins and its propensity to be soluble on overexpression in Escherichia coli.
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Sequence determinants of protein aggregation: tools to increase protein solubility.CyanoPhyChe: a database for physico-chemical properties, structure and biochemical pathway information of cyanobacterial proteinsOctarellin VI: using rosetta to design a putative artificial (β/α)8 proteinFunctional characterization of a small heat shock protein from Mycobacterium lepraeLearning to predict expression efficacy of vectors in recombinant protein production.Sweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression.Prediction and analysis of protein solubility using a novel scoring card method with dipeptide compositionAcalPred: a sequence-based tool for discriminating between acidic and alkaline enzymes.A review of machine learning methods to predict the solubility of overexpressed recombinant proteins in Escherichia coliLarge-scale experimental studies show unexpected amino acid effects on protein expression and solubility in vivo in E. coli.Multiple post-translational modifications affect heterologous protein synthesis.Periscope: quantitative prediction of soluble protein expression in the periplasm of Escherichia coli.Enzyme-linked immunosorbent assay using recombinant SAG1 antigen to detect Toxoplasma gondii-specific immunoglobulin G antibodies in human sera and salivaDiscrimination of soluble and aggregation-prone proteins based on sequence information.Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa.Toxin Fused with SUMO Tag: A New Expression Vector Strategy to Obtain Recombinant Venom Toxins with Easy Tag Removal inside the Bacteria.Current state and recent advances in biopharmaceutical production in Escherichia coli, yeasts and mammalian cells.Bioinformatics approaches for improved recombinant protein production in Escherichia coli: protein solubility prediction.Towards more accurate prediction of protein folding rates: a review of the existing Web-based bioinformatics approaches.mesT, a unique epoxide hydrolase, is essential for optimal growth of Mycobacterium tuberculosis in the presence of styrene oxide.Design strategies to address the effect of hydrophobic epitope on stability and in vitro assembly of modular virus-like particleIdentification of multiple physicochemical and structural properties associated with soluble expression of eukaryotic proteins in cell-free bacterial extracts.Functional characterization of the dimerization domain of the ferric uptake regulator (Fur) of Pseudomonas aeruginosa.Rational identification of aggregation hotspots based on secondary structure and amino acid hydrophobicity.Rare codon content affects the solubility of recombinant proteins in a codon bias-adjusted Escherichia coli strain.Scoring function to predict solubility mutagenesisPaRSnIP: Sequence-Based Protein Solubility Prediction using Gradient Boosting Machine.Characterization of Afp1, an antifreeze protein from the psychrophilic yeast Glaciozyma antarctica PI12.SOLpro: accurate sequence-based prediction of protein solubility.Automatic classification of protein structures using physicochemical parameters.Protein solubility: sequence based prediction and experimental verification.Analysis of high throughput protein expression in Escherichia coli.Expression of a Chimeric Allergen with High Rare Codons Content in Codon Bias-Adjusted Escherichia coli: Escherichia coli BL21 (DE3)-Codon Plus RIL as an Efficient Host.Structural modeling and molecular simulation analysis of HvAP2/EREBP from barley.ESPRESSO: a system for estimating protein expression and solubility in protein expression systems.Correlation Between Protein Primary Structure and Soluble Expression Level of HSA dAb in Escherichia coli.Computational analysis of the amino acid interactions that promote or decrease protein solubilityComputational comparison of two new fusion proteins for multiple sclerosisStrategic single point mutation yields a solvent- and salt-stable transaminase from Virgibacillus sp. in soluble form
P2860
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P2860
Understanding the relationship between the primary structure of proteins and its propensity to be soluble on overexpression in Escherichia coli.
description
2005 nî lūn-bûn
@nan
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
2005年论文
@zh
2005年论文
@zh-cn
name
Understanding the relationship ...... xpression in Escherichia coli.
@ast
Understanding the relationship ...... xpression in Escherichia coli.
@en
type
label
Understanding the relationship ...... xpression in Escherichia coli.
@ast
Understanding the relationship ...... xpression in Escherichia coli.
@en
prefLabel
Understanding the relationship ...... xpression in Escherichia coli.
@ast
Understanding the relationship ...... xpression in Escherichia coli.
@en
P2860
P356
P1433
P1476
Understanding the relationship ...... xpression in Escherichia coli.
@en
P2093
Petety V Balaji
Susan Idicula-Thomas
P2860
P304
P356
10.1110/PS.041009005
P577
2005-02-02T00:00:00Z