about
Protein production and purificationTo fuse or not to fuse: what is your purpose?Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fusedTobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiencyApplication of protein engineering to enhance crystallizability and improve crystal properties.Applications of novel affinity cassette methods: use of peptide fusion handles for the purification of recombinant proteins.Maltose-binding protein enhances secretion of recombinant human granzyme B accompanied by in vivo processing of a precursor MBP fusion protein.Development of the Fc-III tagged protein expression system for protein purification and detection.Improvement of the crystallizability and expression of an RNA crystallization chaperoneOverview of the purification of recombinant proteins.Recombinant Expression and Characterization of α-Conotoxin LvIA in Escherichia coli.Strategies for achieving high-level expression of genes in Escherichia coli.Minimizing a binding domain from protein A.Multimodal protein constructs for herbivore insect control.Towards a recombinant vaccine against diphtheria toxinDesign of an in vivo cleavable disulfide linker in recombinant fusion proteins.In vivo immobilization of fusion proteins on bioplastics by the novel tag BioF.Effects of the Fc-III tag on activity and stability of green fluorescent protein and human muscle creatine kinaseOverview of the purification of recombinant proteins produced in Escherichia coli.Preparation and characterization of a bifunctional aldolase/kinase enzyme: a more efficient biocatalyst for C-C bond formation.Very high-level production and export in Escherichia coli of a cellulose binding domain for use in a generic secretion-affinity fusion system.Impact of an N-terminal Polyhistidine Tag on Protein Thermal Stability.Non-Antibody Scaffolds as Alternative Therapeutic AgentsQuantitation of Transition Metals Using Genetically Engineered Enzymes Carrying Polyhistidine Tails
P2860
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P2860
description
1992 nî lūn-bûn
@nan
1992 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Fusion proteins in biotechnology.
@ast
Fusion proteins in biotechnology.
@en
type
label
Fusion proteins in biotechnology.
@ast
Fusion proteins in biotechnology.
@en
prefLabel
Fusion proteins in biotechnology.
@ast
Fusion proteins in biotechnology.
@en
P2093
P1476
Fusion proteins in biotechnology.
@en
P2093
P304
P356
10.1016/0958-1669(92)90164-E
P577
1992-08-01T00:00:00Z