ArticleBioinformation2018
PROPAB: Computation of Propensities and Other Properties from Segments of 3D structure of Proteins.
Article in Bioinformation, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Salt-bridges in the microenvironment of stable protein structures.Bioinformation · 2020Article
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7 authors.
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Abstract
Residues in allelic positions, in the local segment of aligned sequences of proteins show wide variations. Here, we describe PROPAB that computes the propensity tables for helix, strand and coil types from multiple 3D structure files following ab initio statistical procedure. It also classifies them in range specific and chain specific manners. It further computes percentage composition and physicochemical properties along with residues propensities. It also prepares FASTA files for different segments (helix, strand and coil) in the exact order that they follow in the sequence. Representative analyses on orthologous (homologous across species) proteins demonstrate wide segmental variations of physicochemical properties. Such variations provide insights to relate the adaptation of these proteins in a given functional constraint under diverse environmental conditions. Thus, the program finds applications in the structural and evolutionary analysis of proteins. AVAILABILITY: PROPAB is freely available at http://sourceforge.net/projects/propab/for worldwide user.
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