The Affinity of GXXXG Motifs in Transmembrane Helix-Helix Interactions Is Modulated by Long-range Communication
Open Access
- 1 April 2004
- journal article
- Published by Elsevier
- Vol. 279 (16) , 16591-16597
- https://doi.org/10.1074/jbc.m313936200
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Transmembrane domain mediated self-assembly of major coat protein subunits from Ff bacteriophageJournal of Molecular Biology, 2002
- The GxxxG motif: A framework for transmembrane helix-helix associationJournal of Molecular Biology, 2000
- Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighboring positionsJournal of Molecular Biology, 2000
- Detergents modulate dimerization, but not helicity, of the glycophorin A transmembrane domainJournal of Molecular Biology, 1999
- Changing single side-chains can greatly enhance the resistance of a membrane protein to irreversible inactivationJournal of Molecular Biology, 1999
- The major coat protein of filamentous bacteriophage f1 specifically pairs in the bacterial cytoplasmic membraneJournal of Molecular Biology, 1998
- Helix-helix packing in a membrane-like environmentJournal of Molecular Biology, 1997
- Analysis of Main Chain Torsion Angles in Proteins: Prediction of NMR Coupling Constants for Native and Random Coil ConformationsJournal of Molecular Biology, 1996
- Detergent-solubilized M13 coat protein exists as an asymmetric dimerJournal of Molecular Biology, 1990
- The isolation of a dimer of gene 8 protein of bacteriophage fdJournal of Molecular Biology, 1976