Faculty Opinions recommendation of Optimal data collection for correlated mutation analysis.

Author(s):  
Nathan Baker
2009 ◽  
Vol 74 (3) ◽  
pp. 545-555 ◽  
Author(s):  
Haim Ashkenazy ◽  
Ron Unger ◽  
Yossef Kliger

2010 ◽  
Vol 23 (5) ◽  
pp. 321-326 ◽  
Author(s):  
Haim Ashkenazy ◽  
Yossef Kliger

2005 ◽  
Vol 18 (5) ◽  
pp. 247-253 ◽  
Author(s):  
Orly Noivirt ◽  
Miriam Eisenstein ◽  
Amnon Horovitz

PLoS ONE ◽  
2009 ◽  
Vol 4 (6) ◽  
pp. e5913 ◽  
Author(s):  
Feng Xu ◽  
Pan Du ◽  
Hongbo Shen ◽  
Hairong Hu ◽  
Qi Wu ◽  
...  

2005 ◽  
Vol 14 (05) ◽  
pp. 849-865 ◽  
Author(s):  
YING ZHAO ◽  
GEORGE KARYPIS

Contact map prediction is of great interest for its application in fold recognition and protein 3D structure determination. In this paper we present a contact-map prediction algorithm that employs Support Vector Machines as the machine learning tool and incorporates various features such as sequence profiles and their conservations, correlated mutation analysis based on various amino acid physicochemical properties, and secondary structure. In addition, we evaluated the effectiveness of the different features on contact map prediction for different fold classes. On average, our predictor achieved a prediction accuracy of 0.224 with an improvement over a random predictor of a factor 11.7, which is better than reported studies. Our study showed that predicted secondary structure features play an important roles for the proteins containing beta-structures. Models based on secondary structure features and correlated mutation analysis features produce different sets of predictions. Our study also suggests that models learned separately for different protein fold families may achieve better performance than a unified model.


2018 ◽  
Author(s):  
Miguel Correa Marrero ◽  
Richard G.H. Immink ◽  
Dick de Ridder ◽  
Aalt D.J van Dijk

Predicting residue-residue contacts between interacting proteins is an important problem in bioinformatics. The growing wealth of sequence data can be used to infer these contacts through correlated mutation analysis on multiple sequence alignments of interacting homologs of the proteins of interest. This requires correct identification of pairs of interacting proteins for many species, in order to avoid introducing noise (i.e. non-interacting sequences) in the analysis that will decrease predictive performance. We have designed Ouroboros, a novel algorithm to reduce such noise in intermolecular contact prediction. Our method iterates between weighting proteins according to how likely they are to interact based on the correlated mutations signal, and predicting correlated mutations based on the weighted sequence alignment. We show that this approach accurately discriminates between protein interaction versus noninteraction and simultaneously improves the prediction of intermolecular contact residues compared to a naive application of correlated mutation analysis. Furthermore, the method relaxes the assumption of one-to-one interaction of previous approaches, allowing for the study of many-to-many interactions. Source code and test data are available at www.bif.wur.nl/


Sign in / Sign up

Export Citation Format

Share Document