Protecting role of cosolvents in protein denaturation by SDS: a structural study - Wikidata - wikimedia - TriplyDB

Protecting role of cosolvents in protein denaturation by SDS: a structural study

Protecting role of cosolvents in protein denaturation by SDS: a structural study

http://www.wikidata.org/entity/Q27650741

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PagP Crystallized from SDS/Cosolvent Reveals the Route for Phospholipid Access to the Hydrocarbon Ruler Beyond the detergent effect: a binding site for sodium dodecyl sulfate (SDS) in mammalian apoferritin Towards a universal method for protein refolding: the trimeric beta barrel membrane Omp2a as a test case.Crystallization of lysozyme with (R)-, (S)- and (RS)-2-methyl-2,4-pentanediol.Complexes of native ubiquitin and dodecyl sulfate illustrate the nature of hydrophobic and electrostatic interactions in the binding of proteins and surfactants.2-Methyl-2,4-pentanediol (MPD) boosts as detergent-substitute the performance of ß-barrel hybrid catalyst for phenylacetylene polymerization.Refolding of SDS-denatured proteins using amphipathic cosolvents and osmolytes.Unravelling the mechanisms of a protein refolding process based on the association of detergents and co-solvents.Purification and characterization of an amyloglucosidase from an ericoid mycorrhizal fungus (Leohumicola incrustata)

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P2860

Protecting role of cosolvents in protein denaturation by SDS: a structural study

http://www.wikidata.org/entity/Q27650741

description

2008 nî lūn-bûn

@nan

2008 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Protecting role of cosolvents in protein denaturation by SDS: a structural study

@ast

Protecting role of cosolvents in protein denaturation by SDS: a structural study

@en

Protecting role of cosolvents in protein denaturation by SDS: a structural study

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type

label

Protecting role of cosolvents in protein denaturation by SDS: a structural study

@ast

Protecting role of cosolvents in protein denaturation by SDS: a structural study

@en

Protecting role of cosolvents in protein denaturation by SDS: a structural study

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prefLabel

Protecting role of cosolvents in protein denaturation by SDS: a structural study

@ast

Protecting role of cosolvents in protein denaturation by SDS: a structural study

@en

Protecting role of cosolvents in protein denaturation by SDS: a structural study

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BMC Structural Biology

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Protecting role of cosolvents in protein denaturation by SDS: a structural study

@en

P2093

Catherine Michaux

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

Jenny Pouyez

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

P2860

Crystallization, structure solution and refinement of hen egg-white lysozyme at pH 8.0 in the presence of MPD

Coot: model-building tools for molecular graphics

Likelihood-enhanced fast rotation functions

SHELXL: high-resolution refinement

Refinement of macromolecular structures by the maximum-likelihood method

XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

Effect of alcohols on protein hydration: crystallographic analysis of hen egg-white lysozyme in the presence of alcohols.

Protein unfolding in detergents: effect of micelle structure, ionic strength, pH, and temperature.

A structural basis for the interaction of urea with lysozyme.

An overview on 2-methyl-2,4-pentanediol in crystallization and in crystals of biological macromolecules.

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29

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scholarly article

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10.1186/1472-6807-8-29

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1

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8

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Gilbert G Privé

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2008-06-03T00:00:00Z

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51399128

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1003437472

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18522744

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structural biology

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2429906

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