Improving the resistance of a eukaryotic β-barrel protein to thermal and chemical perturbations. - Wikidata - awgldk - TriplyDB

Improving the resistance of a eukaryotic β-barrel protein to thermal and chemical perturbations.

Improving the resistance of a eukaryotic β-barrel protein to thermal and chemical perturbations.

http://www.wikidata.org/entity/Q30155492

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Outer membrane protein design.Evidence of Distinct Channel Conformations and Substrate Binding Affinities for the Mitochondrial Outer Membrane Protein Translocase Pore Tom40.Weakly stable regions and protein-protein interactions in beta-barrel membrane proteins Engineered oligomerization state of OmpF protein through computational design decouples oligomer dissociation from unfolding.Predicting three-dimensional structures of transmembrane domains of β-barrel membrane proteins.An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins.High-resolution structure prediction of β-barrel membrane proteins.

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Improving the resistance of a eukaryotic β-barrel protein to thermal and chemical perturbations.

http://www.wikidata.org/entity/Q30155492

description

2011 nî lūn-bûn

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2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հուլիսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Improving the resistance of a ...... al and chemical perturbations.

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Improving the resistance of a ...... al and chemical perturbations.

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Improving the resistance of a ...... al and chemical perturbations.

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J.JMB.2011.07.054

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Journal of Molecular Biology

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Improving the resistance of a ...... al and chemical perturbations.

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Dennis Gessmann

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

Dirk Linke

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

Frauke Mager

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

Jie Liang

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

Sara Weirich

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

Stephan Nussberger

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

Thomas Arnold

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P2860

Characterization of rat TOM40, a central component of the preprotein translocase of the mitochondrial outer membrane

Identification of Tom5 and Tom6 in the preprotein translocase complex of human mitochondrial outer membrane

Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria

Structure of the human voltage-dependent anion channel

High-resolution crystal structure of an artificial (betaalpha)(8)-barrel protein designed from identical half-barrels

Enhancing the stability and solubility of the glucocorticoid receptor ligand-binding domain by high-throughput library screening

Stability of trimeric OmpF porin: the contributions of the latching loop L2

Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins [see comment].

Structure and evolution of mitochondrial outer membrane proteins of beta-barrel topology

Protein stability curves

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10.1016/J.JMB.2011.07.054

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