Life at the border: adaptation of proteins to anisotropic membrane environment.

Irina D. Pogozheva, Henry I. Mosberg, Andrei L. Lomize
Published 2014 in
Protein science : a publication of the Protein…

Abstract

This review discusses main features of transmembrane (TM) proteins which distinguish them from water-soluble proteins and allow their adaptation to the anisotropic membrane environment. We overview the structural limitations on membrane protein architecture, spatial arrangement of proteins in membranes and their intrinsic hydrophobic thickness, co… (More)

DOI: 10.1002/pro.2508

Photophysical properties of hydroxyphenyl benzazoles and their applications as fluorescent probes to study local environment in DNA, protein and lipid.

Saba A J Sulaiman, Ghalia S Al-Rasbi, Osama K Abou-Zied
Luminescence : the journal of biological and…
2016

Life at the border: adaptation of proteins to anisotropic membrane environment.

Abstract

Topics

14 Figures and Tables

Cited By

Outer membrane protein folding from an energy landscape perspective

Photophysical properties of hydroxyphenyl benzazoles and their applications as fluorescent probes to study local environment in DNA, protein and lipid.

Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.

References

High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population.

Mitochondrial alterations in apoptosis.

Structural basis of Sec-independent membrane protein insertion by YidC.

Structure determination of α-helical membrane proteins by solution-state NMR: emphasis on retinal proteins.

Structures of the Sec61 complex engaged in nascent peptide translocation or membrane insertion.

X-ray structure, thermodynamics, elastic properties and MD simulations of cardiolipin/dimyristoylphosphatidylcholine mixed membranes.

Charge pair interactions in transmembrane helices and turn propensity of the connecting sequence promote helical hairpin insertion.

Common folds and transport mechanisms of secondary active transporters.

Crystal structure and functional mechanism of a human antimicrobial membrane channel.

Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis.

Slides referencing similar topics

Life at the border: adaptation of proteins to anisotropic membrane environment.

Abstract

Topics

14 Figures and Tables

Cited By

Outer membrane protein folding from an energy landscape perspective

Photophysical properties of hydroxyphenyl benzazoles and their applications as fluorescent probes to study local environment in DNA, protein and lipid.

Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.

References

High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population.

Mitochondrial alterations in apoptosis.

Structural basis of Sec-independent membrane protein insertion by YidC.

Structure determination of α-helical membrane proteins by solution-state NMR: emphasis on retinal proteins.

Structures of the Sec61 complex engaged in nascent peptide translocation or membrane insertion.

X-ray structure, thermodynamics, elastic properties and MD simulations of cardiolipin/dimyristoylphosphatidylcholine mixed membranes.

Charge pair interactions in transmembrane helices and turn propensity of the connecting sequence promote helical hairpin insertion.

Common folds and transport mechanisms of secondary active transporters.

Crystal structure and functional mechanism of a human antimicrobial membrane channel.

Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis.

Similar Papers

Slides referencing similar topics