Phil Bradley
Massachusetts Institute of Technology
7 Papers
2 Citations
Phil Bradley is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Structural motif & Biology. The author has an hindex of 6, co-authored 7 publications. Previous affiliations of Phil Bradley include University College Dublin.
Chat about Author
Papers
betawrap: Successful prediction of parallel β-helices from primary sequence reveals an association with many microbial pathogens
TL;DR: A computational approach is presented that predicts the right-handed parallel β-helix supersecondary structural motif in primary amino acid sequences by using β-strand interactions learned from non-β-helIX structures to generate interstrand pairwise correlations from a processive sequence wrap.
132
Predicting the beta-helix fold from protein sequence data.
TL;DR: A method is presented that uses beta-strand interactions to predict the parallel right-handed beta-helix super-secondary structural motif in protein sequences and may generalize to other beta-structures for which strand topology and profiles of residue accessibility are well conserved.
Cellular Automata with Rare Events; Resolution of an Outstanding Problem in the Bootstrap Percolation Model
Paolo De Gregorio,Aonghus Lawlor,Phil Bradley,Kenneth A. Dawson +3 more
- 25 Oct 2004
TL;DR: A new importance-sampling procedure in simulation, based on rare events around “holes”, is introduced, which enables credible comparisons between theory and simulation in the accessible density range.
2
Clarification of the bootstrap percolation paradox.
TL;DR: By framing a new theory in terms of paths or processes that lead to emptying of the lattice, it is possible to obtain credible comparisons between theory and simulation in the accessible density range.
Predicting the b-helix fold from protein sequence data
Phil Bradley,Lenore J. Cowen,Matthew Menke,Jonathan King,Bonnie Berger +4 more
- 22 Apr 2001
TL;DR: A method is presented that uses β-strand interactions to predict the right-handed β-helix super-secondary structural motif in protein sequences, and is shown to score known β-helices above non-β- helices in the Protein Data Bank in cross-validation.