Purification of Proteins Fused to Maltose-Binding Protein.

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Robust Production, Crystallization, Structure Determination, and Analysis of [Fe-S] Proteins: Uncovering Control of Electron Shuttling and Gating in the Respiratory Metabolism of Molybdopterin Guanine Dinucleotide Enzymes.

P2860

Q55689317-FBAD68DC-584D-49A1-9D5D-FA3425355583

P2860

Purification of Proteins Fused to Maltose-Binding Protein.

Item

http://www.wikidata.org/entity/Q51404677

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2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Purification of Proteins Fused to Maltose-Binding Protein.

@en

Purification of Proteins Fused to Maltose-Binding Protein.

@nl

type

Item

label

Purification of Proteins Fused to Maltose-Binding Protein.

@en

Purification of Proteins Fused to Maltose-Binding Protein.

@nl

prefLabel

Purification of Proteins Fused to Maltose-Binding Protein.

@en

Purification of Proteins Fused to Maltose-Binding Protein.

@nl

P1476

Purification of Proteins Fused to Maltose-Binding Protein.

@en

P2093

Mario Lebendiker

http://www.w3.org/2001/XMLSchema#string

Tsafi Danieli

http://www.w3.org/2001/XMLSchema#string

P2860

Controlled intracellular processing of fusion proteins by TEV protease

Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency

A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1

Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors

Inhibition of tobacco etch virus protease activity by detergents.

Simultaneous determination of protein aggregation, degradation, and absolute molecular weight by size exclusion chromatography-multiangle laser light scattering.

Methods for protein characterization by mass spectrometry, thermal shift (ThermoFluor) assay, and multiangle or static light scattering.

The ability to enhance the solubility of its fusion partners is an intrinsic property of maltose-binding protein but their folding is either spontaneous or chaperone-mediated

Crystal structures of fusion proteins with large-affinity tags.

Recombinant protein folding and misfolding in Escherichia coli.

P304

257-273

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1007/978-1-4939-6412-3_13

http://www.w3.org/2001/XMLSchema#string

P407

English

P478

1485

http://www.w3.org/2001/XMLSchema#string

P577

2017-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

27730557

http://www.w3.org/2001/XMLSchema#string

Purification of Proteins Fused to Maltose-Binding Protein.

about

P2860

P2860

Purification of Proteins Fused to Maltose-Binding Protein.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P478

P577

P698