DMCA
Analysis and Prediction of Helix–Helix Interactions in Membrane Channels and Transporters
BibTeX
@MISC{Hildebr_analysisand,
author = {Peter Werner Hildebr and Stephan Lorenzen and Andrean Goede and Robert Preissner},
title = {Analysis and Prediction of Helix–Helix Interactions in Membrane Channels and Transporters},
year = {}
}
Share
 |
 |
 |
 |
||
OpenURL
Abstract
ABSTRACT Membrane proteins span a large variety of different functions such as cell-surface re-ceptors, redox proteins, ion channels, and transport-ers. Proteins with functional pores show different characteristics of helix–helix packing as other helical membrane proteins. We found that the helix–helix contacts of 13 nonhomologous high-resolution struc-tures of membrane channels and transporters are mainly accomplished by weakly polar amino acids (G> S> T> F) that preferably create contacts every fourth residue, typical for right-handed helix cross-ings. There is a strong correlation between the now available biological hydrophobicity scale and the pro-pensities of the weakly polar and hydrophobic resi-dues to be buried at helix–helix interfaces or to be
Keyphrases
membrane channel helix helix interaction redox protein nonhomologous high-resolution struc-tures abstract membrane functional pore fourth residue weakly polar helical membrane protein cell-surface re-ceptors ion channel large variety different function helix helix interface helix helix packing strong correlation weakly polar amino acid helix helix contact available biological hydrophobicity scale different characteristic right-handed helix cross-ings hydrophobic resi-dues
