Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10231980 | Computational Biology and Chemistry | 2005 | 8 Pages |
Abstract
A deterministic algorithm for enumeration of transmembrane protein folds is presented. Using a set of sparse pairwise atomic distance constraints (such as those obtained from chemical cross-linking, FRET, or dipolar EPR experiments), the algorithm performs an exhaustive search of secondary structure element packing conformations distributed throughout the entire conformational space. The end result is a set of distinct protein conformations, which can be scored and refined as part of a process designed for computational elucidation of transmembrane protein structures.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
W. Michael Brown, Jean-Loup Faulon, Ken Sale,