Structure calculation strategies for helical membrane proteins; a comparison study
| dc.creator | Stoica, Ileana | |
| dc.date | 2005-05-06 | |
| dc.date | 2005-08-21 | |
| dc.date.accessioned | 2026-07-07T05:59:15Z | |
| dc.date.available | 2026-07-07T05:59:15Z | |
| dc.description | Structure predictions of helical membrane proteins have been designed to take advantage of the structural autonomy of secondary structure elements, as postulated by the two-stage model of Engelman and Popot. In this context, we investigate structure calculation strategies for two membrane proteins with different functions, sizes, aminoacid compositions, and topologies: the glycophorin A homodimer (a paradigm for close inter-helical packing in membrane proteins) and aquaporin (a channel protein). Our structure calculations are based on two alternative folding schemes: a one-step simulated annealing from an extended chain conformation, and a two-step procedure inspired by the grid-search methods traditionally used in membrane protein predictions. In this framework, we investigate rationales for the utilization of sparse NMR data such as distance-based restraints and residual dipolar couplings in structure calculations of helical membrane proteins. | |
| dc.identifier | https://arxiv.org/abs/q-bio/0505014 | |
| dc.identifier | http://arxiv.org/abs/q-bio/0505014 | |
| dc.identifier.uri | http://salesiana.dossiersoluciones.com/handle/123456789/88610 | |
| dc.subject | Biomolecules | |
| dc.title | Structure calculation strategies for helical membrane proteins; a comparison study | |
| dc.type | text |