Sequence motifs, polar interactions and conformational changes in helical membrane proteins
- 16 July 2003
- journal article
- review article
- Published by Elsevier in Current Opinion in Structural Biology
- Vol. 13 (4) , 412-417
- https://doi.org/10.1016/s0959-440x(03)00102-7
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- Functional Role of Cα–H⋯O Hydrogen Bonds Between Transmembrane α-Helices in Photosystem IJournal of Molecular Biology, 2003
- Standardizing the Free Energy Change of Transmembrane Helix–Helix InteractionsJournal of Molecular Biology, 2002
- Opening the KcsA K+ Channel: Tryptophan Scanning and Complementation Analysis Lead to Mutants with Altered GatingBiochemistry, 2002
- The open pore conformation of potassium channelsNature, 2002
- Crystal structure and mechanism of a calcium-gated potassium channelNature, 2002
- Transmembrane domain mediated self-assembly of major coat protein subunits from Ff bacteriophageJournal of Molecular Biology, 2002
- Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain11Edited by B. HollandJournal of Molecular Biology, 2001
- Structure and function in bacteriorhodopsin: the role of the interhelical loops in the folding and stability of bacteriorhodopsinJournal of Molecular Biology, 2001
- 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
- The Structure of the Potassium Channel: Molecular Basis of K + Conduction and SelectivityScience, 1998