Positively and negatively charged residues have different effects on the position in the membrane of a model transmembrane helix
- 11 December 1998
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 284 (4), 1177-1183
- https://doi.org/10.1006/jmbi.1998.2218
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Proline-induced disruption of a transmembrane α-helix in its natural environmentJournal of Molecular Biology, 1998
- fd coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helixJournal of Molecular Biology, 1997
- The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase.The Journal of cell biology, 1994
- Proton migration along the membrane surface and retarded surface to bulk transferNature, 1994
- Influence of proline residues on protein conformationJournal of Molecular Biology, 1991
- Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineeringProtein Engineering, Design and Selection, 1990
- Context effects and inefficient initiation at non-AUG codons in eucaryotic cell-free translation systems.Molecular and Cellular Biology, 1989
- Mitochondrial targeting sequences why ‘non‐amphiphilic’ peptides may still be amphiphilicFEBS Letters, 1988
- Helix geometry in proteinsJournal of Molecular Biology, 1988
- Rapid and efficient site-specific mutagenesis without phenotypic selection.Proceedings of the National Academy of Sciences, 1985