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pro vyhledávání: '"Kanaka Durga Kedarisetti"'
Publikováno v:
Bioinformatics and Biology Insights, Vol 2008, Iss 2, Pp 133-144 (2008)
Externí odkaz:
https://doaj.org/article/eb4bffbd85cf445f8c3bf7845f1e9105
Publikováno v:
Bioinformatics and Biology Insights, Vol 2, Pp 133-144 (2008)
The exact mechanisms of prion misfolding and factors that predispose an individual to prion diseases are largely unknown. Our approach to identifying candidate factors in-silico relies on contrasting the C-terminal domain of PrPC sequences from two g
Externí odkaz:
https://doaj.org/article/0ad6dd2b0e5e46e18fbc8b05b07d9934
Autor:
Marcin J. Mizianty, Kanaka Durga Kedarisetti, Wojciech Stach, Tuo Zhang, Lukasz Kurgan, Ke Chen, Hua Zhang, Qingbo Bao
Publikováno v:
Briefings in Bioinformatics. 12:672-688
Sequence-based prediction of protein secondary structure (SS) enjoys wide-spread and increasing use for the analysis and prediction of numerous structural and functional characteristics of proteins. The lack of a recent comprehensive and large-scale
Autor:
Kanaka Durga Kedarisetti, Lukasz Kurgan, Marcin J. Mizianty, Ke Chen, Wojciech Stach, Fatemeh Miri Disfani
Publikováno v:
Bioinformatics
Motivation: Intrinsically disordered proteins play a crucial role in numerous regulatory processes. Their abundance and ubiquity combined with a relatively low quantity of their annotations motivate research toward the development of computational mo
Publikováno v:
Journal of bioinformatics and computational biology. 9(1)
Accurate identification of strand residues aids prediction and analysis of numerous structural and functional aspects of proteins. We propose a sequence-based predictor, BETArPRED, which improves prediction of strand residues and β-strand segments.
Publikováno v:
Bioinformatics and Biology Insights
Bioinformatics and Biology Insights, Vol 2, Pp 133-144 (2008)
Bioinformatics and Biology Insights, Vol 2 (2008)
Bioinformatics and Biology Insights, Vol 2008, Iss 2, Pp 133-144 (2008)
Bioinformatics and Biology Insights, Vol 2, Pp 133-144 (2008)
Bioinformatics and Biology Insights, Vol 2 (2008)
Bioinformatics and Biology Insights, Vol 2008, Iss 2, Pp 133-144 (2008)
The exact mechanisms of prion misfolding and factors that predispose an individual to prion diseases are largely unknown. Our approach to identifying candidate factors in-silico relies on contrasting the C-terminal domain of PrPC sequences from two g
Publikováno v:
The protein journal. 25(7-8)
Characterizing and classifying regularities in protein structure is an important element in uncovering the mechanisms that regulate protein structure, function and evolution. Recent research concentrates on analysis of structural motifs that can be u
Publikováno v:
CIBCB
Protein structure prediction is one of the core research areas in bioinformatics. This paper addresses the protein secondary structure prediction problem for the twilight zone proteins, which are characterized by low, about 25% homology to the sets o
Publikováno v:
Biochemical and biophysical research communications. 348(3)
Structural class characterizes the overall folding type of a protein or its domain. A number of computational methods have been proposed to predict structural class based on primary sequences; however, the accuracy of these methods is strongly affect
Publikováno v:
Computational Biology and Chemistry. 30:393-394
Protein structural class describes the overall folding type of a protein or its domain. A number of methods were developed to predict protein structural class based on its primary sequence. The homology of the predicted sequences with respect to the