0000000000205457
AUTHOR
David Gilbert
showing 4 related works from this author
Pattern Matching and Pattern Discovery Algorithms for Protein Topologies
2001
We describe algorithms for pattern-matching and pattern-learning in TOPS diagrams (formal descriptions of protein topologies). These problems can be reduced to checking for subgraph isomorphism and finding maximal common subgraphs in a restricted class of ordered graphs. We have developed a subgraph isomorphism algorithm for ordered graphs, which performs well on the given set of data. The maximal common subgraph problem then is solved by repeated subgraph extension and checking for isomorphisms. Despite its apparent inefficiency, this approach yields an algorithm with time complexity proportional to the number of graphs in the input set and is still practical on the given set of data. As a…
Gene Duplication Models and Reconstruction of Gene Regulatory Network Evolution from Network Structure
2016
The work was supported by Latvian Council of Science grant 258/2012 and Latvian State Research programme project NexIT (2014-2017).
A computer system to perform structure comparison using TOPS representations of protein structure
2001
We describe the design and implementation of a fast topology-based method for protein structure comparison. The approach uses the TOPS topological representation of protein structure, aligning two structures using a common discovered pattern and generating measure of distance derived from an insert score. Heavy use is made of a constraint-based pattern-matching algorithm for TOPS diagrams that we have designed and described elsewhere (Bioinformatics 15(4) (1999) 317). The comparison system is maintained at the European Bioinformatics Institute and is available over the Web at tops.ebi.ac.uk/tops. Users submit a structure description in Protein Data Bank (PDB) format and can compare it with …
Assessment of the probabilities for evolutionary structural changes in protein folds.
2007
Abstract Motivation: The evolution of protein sequences can be described by a stepwise process, where each step involves changes of a few amino acids. In a similar manner, the evolution of protein folds can be at least partially described by an analogous process, where each step involves comparatively simple changes affecting few secondary structure elements. A number of such evolution steps, justified by biologically confirmed examples, have previously been proposed by other researchers. However, unlike the situation with sequences, as far as we know there have been no attempts to estimate the comparative probabilities for different kinds of such structural changes. Results: We have tried …