Docking with PIPER and refinement with SDU in rounds 6-11 of CAPRI

Our approach to protein–protein docking includes three main steps. First we run PIPER, a new rigid body docking program. PIPER is based on the Fast Fourier Transform (FFT) correlation approach that has been extended to use pairwise interactions potentials, thereby substantially increasing the number...

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Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2007-12, Vol.69 (4), p.734-742
Main Authors: Shen, Yang, Brenke, Ryan, Kozakov, Dima, Comeau, Stephen R., Beglov, Dmitri, Vajda, Sandor
Format: Article
Language:English
Subjects:
Algorithms
Cluster Analysis
clustering
Computational Biology - methods
Computer Simulation
DARS pairwise potential
Databases, Protein
energy funnel
Escherichia coli - metabolism
fast Fourier transform
Fourier Analysis
global optimization
Models, Statistical
Monte Carlo Method
Protein Binding
Protein Conformation
protein docking by PIPER
Protein Interaction Mapping
Proteins - chemistry
Proteomics - methods
refinement by SDU
semidefinite programming
Software
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Summary:Our approach to protein–protein docking includes three main steps. First we run PIPER, a new rigid body docking program. PIPER is based on the Fast Fourier Transform (FFT) correlation approach that has been extended to use pairwise interactions potentials, thereby substantially increasing the number of near‐native structures generated. The interaction potential is also new, based on the DARS (Decoys As the Reference State) principle. In the second step, the 1000 best energy conformations are clustered, and the 30 largest clusters are retained for refinement. Third, the conformations are refined by a new medium‐range optimization method SDU (Semi‐Definite programming based Underestimation). SDU has been developed to locate global minima within regions of the conformational space in which the energy function is funnel‐like. The method constructs a convex quadratic underestimator function based on a set of local energy minima, and uses this function to guide future sampling. The combined method performed reliably without the direct use of biological information in most CAPRI problems that did not require homology modeling, providing acceptable predictions for targets 21, and medium quality predictions for targets 25 and 26. Proteins 2007. © 2007 Wiley‐Liss, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.21754