Analysis and refinement of criteria for predicting the structure and relative orientations of transmembranal helical domains
- 1 April 1992
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 62 (1) , 107-109
- https://doi.org/10.1016/s0006-3495(92)81794-0
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- The influence of proline residues on α‐helical structurePublished by Wiley ,2001
- Proline residues in transmembrane helixes: structural or dynamic role?Biochemistry, 1991
- Crystal structure of [Leu1]zervamicin, a membrane ion-channel peptide: implications for gating mechanisms.Proceedings of the National Academy of Sciences, 1991
- Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopyJournal of Molecular Biology, 1990
- The prediction of transmembrane protein sequences and their conformation: an evaluationTrends in Biochemical Sciences, 1990
- The structure of bacteriorhodopsin and its relevance to the visual opsins and other seven-helix G-protein coupled receptorsPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1990
- Amphipathic helix motif: Classes and propertiesProteins-Structure Function and Bioinformatics, 1990
- The Photosynthetic Reaction Center from the Purple Bacterium Rhodopseudomonas viridisScience, 1989
- Proline‐induced constraints in α‐helicesBiopolymers, 1987
- Path of the polypeptide in bacteriorhodopsin.Proceedings of the National Academy of Sciences, 1980