PROTINFO: secondary and tertiary protein structure prediction

Tertiary protein structure prediction in silico is currently a challenging problem in Structural Bioinformatics and can be classified according to the computational complexity theory as an NP-hard problem. Determining the 3-D structure of a protein is both experimentally expensive, and time-consuming. The agent-based paradigm has been shown a useful technique for the applications that have repetitive and time-consuming activities, knowledge share and management, such as integration of different knowledge sources and modeling of complex systems, supporting a great variety of domains. This chapter provides an integrated view and insights about the protein structure prediction area concerned to the usage, application and implementation of multi-agent systems to predict the protein structures or to support and coordinate the existing predictors, as well as it is advantages, issues, needs, and demands. It is noteworthy that there is a great need for works related to multi-agent and agent-based paradigms applied to the problem due to their excellent suitability to the problem.

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Multi-Agent Systems in Three-Dimensional Protein Structure Prediction

Biotechnology ◽

10.4018/978-1-5225-8903-7.ch040 ◽

2019 ◽

pp. 1031-1068

Author(s):

Leonardo de Lima Corrêa ◽

Márcio Dorn

Keyword(s):

Protein Structure ◽

Protein Structure Prediction ◽

Structure Prediction ◽

Protein Structures ◽

Three Dimensional ◽

Multi Agent Systems ◽

Agent Based ◽

Agent Systems ◽

Tertiary Protein Structure ◽

Multi Agent

Tertiary protein structure prediction in silico is currently a challenging problem in Structural Bioinformatics and can be classified according to the computational complexity theory as an NP-hard problem. Determining the 3-D structure of a protein is both experimentally expensive, and time-consuming. The agent-based paradigm has been shown a useful technique for the applications that have repetitive and time-consuming activities, knowledge share and management, such as integration of different knowledge sources and modeling of complex systems, supporting a great variety of domains. This chapter provides an integrated view and insights about the protein structure prediction area concerned to the usage, application and implementation of multi-agent systems to predict the protein structures or to support and coordinate the existing predictors, as well as it is advantages, issues, needs, and demands. It is noteworthy that there is a great need for works related to multi-agent and agent-based paradigms applied to the problem due to their excellent suitability to the problem.

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Sequence Specific Dihedral Angle Distribution: Application in Protein Structure Prediction and Evaluation

Plant Tissue Culture and Biotechnology ◽

10.3329/ptcb.v19i2.5439 ◽

1970 ◽

Vol 19 (2) ◽

pp. 217-226

Author(s):

S. M. Minhaz Ud-Dean ◽

Mahdi Muhammad Moosa

Keyword(s):

Protein Structure ◽

Dihedral Angle ◽

Protein Structure Prediction ◽

Structure Prediction ◽

Protein Structures ◽

Angle Distribution ◽

Ramachandran Plot ◽

Specific Data ◽

Specific Distribution ◽

Structure Evaluation

Protein structure prediction and evaluation is one of the major fields of computational biology. Estimation of dihedral angle can provide information about the acceptability of both theoretically predicted and experimentally determined structures. Here we report on the sequence specific dihedral angle distribution of high resolution protein structures available in PDB and have developed Sasichandran, a tool for sequence specific dihedral angle prediction and structure evaluation. This tool will allow evaluation of a protein structure in pdb format from the sequence specific distribution of Ramachandran angles. Additionally, it will allow retrieval of the most probable Ramachandran angles for a given sequence along with the sequence specific data. Key words: Torsion angle, φ-ψ distribution, sequence specific ramachandran plot, Ramasekharan, protein structure appraisal D.O.I. 10.3329/ptcb.v19i2.5439 Plant Tissue Cult. & Biotech. 19(2): 217-226, 2009 (December)

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