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Deletion variants of Neurospora mitochondrial porin: electrophysiological and spectroscopic analysis.

Deletion variants of Neurospora mitochondrial porin: electrophysiological and spectroscopic analysis.

http://www.wikidata.org/entity/Q30159897

about

The 3D structures of VDAC represent a native conformation β-Barrel mobility underlies closure of the voltage-dependent anion channel The evolutionary history of mitochondrial porins.Origami in outer membrane mimetics: correlating the first detailed images of refolded VDAC with over 20 years of biochemical data.VDAC structure, selectivity, and dynamics.The influence of sterols on the conformation of recombinant mitochondrial porin in detergent.Two-step folding of recombinant mitochondrial porin in detergent.Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.A deletion variant partially complements a porin-less strain of Neurospora crassa.

P2860

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P2860

Deletion variants of Neurospora mitochondrial porin: electrophysiological and spectroscopic analysis.

http://www.wikidata.org/entity/Q30159897

description

2006 nî lūn-bûn

@nan

2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի փետրվարին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Deletion variants of Neurospor ...... al and spectroscopic analysis.

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Deletion variants of Neurospor ...... al and spectroscopic analysis.

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type

label

Deletion variants of Neurospor ...... al and spectroscopic analysis.

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Deletion variants of Neurospor ...... al and spectroscopic analysis.

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prefLabel

Deletion variants of Neurospor ...... al and spectroscopic analysis.

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Deletion variants of Neurospor ...... al and spectroscopic analysis.

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BIOPHYSJ.105.072520

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Biophysical Journal

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Deletion variants of Neurospor ...... al and spectroscopic analysis.

@en

P2093

Elke Maier

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

Greg Runke

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

William A T Summers

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P2860

Structure of outer membrane protein A transmembrane domain by NMR spectroscopy

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

Studies on transformation of Escherichia coli with plasmids

The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria.

Bacterial expression and characterization of the mitochondrial outer membrane channel. Effects of n-terminal modifications.

Lysine residues at positions 234 and 236 in yeast porin are involved in its assembly into the mitochondrial outer membrane.

Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins

Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues

Biogenesis of beta-barrel membrane proteins of mitochondria.

A synthetic peptide forms voltage-gated porin-like ion channels in lipid bilayer membranes.

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3155-3164

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scholarly article

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9

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90

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Deborah A. Court

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2006-02-24T00:00:00Z

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7276528

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electrophysiology

outer mitochondrial membrane protein porin

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1432131

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