9 research outputs found
Maximum Cliques in Protein Structure Comparison
Computing the similarity between two protein structures is a crucial task in
molecular biology, and has been extensively investigated. Many protein
structure comparison methods can be modeled as maximum clique problems in
specific k-partite graphs, referred here as alignment graphs. In this paper, we
propose a new protein structure comparison method based on internal distances
(DAST) which is posed as a maximum clique problem in an alignment graph. We
also design an algorithm (ACF) for solving such maximum clique problems. ACF is
first applied in the context of VAST, a software largely used in the National
Center for Biotechnology Information, and then in the context of DAST. The
obtained results on real protein alignment instances show that our algorithm is
more than 37000 times faster than the original VAST clique solver which is
based on Bron & Kerbosch algorithm. We furthermore compare ACF with one of the
fastest clique finder, recently conceived by Ostergard. On a popular benchmark
(the Skolnick set) we observe that ACF is about 20 times faster in average than
the Ostergard's algorithm
Towards Reliable Automatic Protein Structure Alignment
A variety of methods have been proposed for structure similarity calculation,
which are called structure alignment or superposition. One major shortcoming in
current structure alignment algorithms is in their inherent design, which is
based on local structure similarity. In this work, we propose a method to
incorporate global information in obtaining optimal alignments and
superpositions. Our method, when applied to optimizing the TM-score and the GDT
score, produces significantly better results than current state-of-the-art
protein structure alignment tools. Specifically, if the highest TM-score found
by TMalign is lower than (0.6) and the highest TM-score found by one of the
tested methods is higher than (0.5), there is a probability of (42%) that
TMalign failed to find TM-scores higher than (0.5), while the same probability
is reduced to (2%) if our method is used. This could significantly improve the
accuracy of fold detection if the cutoff TM-score of (0.5) is used.
In addition, existing structure alignment algorithms focus on structure
similarity alone and simply ignore other important similarities, such as
sequence similarity. Our approach has the capacity to incorporate multiple
similarities into the scoring function. Results show that sequence similarity
aids in finding high quality protein structure alignments that are more
consistent with eye-examined alignments in HOMSTRAD. Even when structure
similarity itself fails to find alignments with any consistency with
eye-examined alignments, our method remains capable of finding alignments
highly similar to, or even identical to, eye-examined alignments.Comment: Peer-reviewed and presented as part of the 13th Workshop on
Algorithms in Bioinformatics (WABI2013
Capturing Long-Term Dependencies for Protein Secondary Structure Prediction
Abstract. Bidirectional recurrent neural network(BRNN) is a noncausal system that captures both upstream and downstream information for protein secondary structure prediction. Due to the problem of vanishing gradients, the BRNN can not learn remote information efficiently. To limit this problem, we propose segmented memory recurrent neural network(SMRNN) and use SMRNNs to replace the standard RNNs in BRNN. The resulting architecture is called bidirectional segmented-memory recurrent neural network(BSMRNN). Our experiment with BSMRNN for protein secondary structure prediction on the RS126 set indicates improvement in the prediction accuracy.
Sur les grands massifs karstiques d'Andalousie : Manuel C. Pezzi
Nicod Jean. Sur les grands massifs karstiques d'Andalousie : Manuel C. Pezzi . In: Annales de Géographie, t. 88, n°490, 1979. pp. 753-755