Download e-book for iPad: Advances in Computational Biology: Proceedings of the 2nd by Ivan Mura (auth.), Luis F. Castillo, Marco Cristancho,

By Ivan Mura (auth.), Luis F. Castillo, Marco Cristancho, Gustavo Isaza, Andrés Pinzón, Juan Manuel Corchado Rodríguez (eds.)

ISBN-10: 3319015672

ISBN-13: 9783319015675

ISBN-10: 3319015680

ISBN-13: 9783319015682

This quantity compiles accredited contributions for the 2d variation of the Colombian Computational Biology and Bioinformatics Congress CCBCOL, after a rigorous assessment method within which fifty four papers have been accredited for book from 119 submitted contributions. Bioinformatics and Computational Biology are parts of data that experience emerged because of advances that experience taken position within the organic Sciences and its integration with details Sciences. the growth of initiatives regarding the learn of genomes has led the best way within the construction of massive quantities of series info which has to be prepared, analyzed and kept to appreciate phenomena linked to dwelling organisms relating to their evolution, habit in numerous ecosystems, and the advance of purposes that may be derived from this analysis.

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Additional info for Advances in Computational Biology: Proceedings of the 2nd Colombian Congress on Computational Biology and Bioinformatics (CCBCOL)

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4, 187–217 (1983) 22. : Achieving reliability and high accuracy in automated protein docking: Cluspro, PIPER, SDU, and stability analysis in CAPRI rounds 13–19. Proteins: Structure, Function, and Bioinformatics 78, 3124–3130 (2010) Analysis of Binding Residues between PDGF-BB and Epidermal Growth Factor Receptor 39 23. : MolProbity: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Research 32, W615–W619 (2004) 24. : PROCHECK: validation of protein structure coordnates.

The simplest viruses that display icosahedral symmetry have 60 copies of a single coat protein subunit (single gene product) arranged in equivalent (identical) environments related by fivefold, three-fold, and twofold axes of symmetry. In addition, viral capsids provide an excellent resource for studying protein-protein interactions in homo-oligomers that form symmetric closed shells, since association and self-assembly of the capsid protein subunits are common to all viruses. Analysis of protein-protein interactions in viral capsids may reveal the molecular principles of recognition and self-assembly and the nature of interactions that lead to capsid formation, given that interactions between the coat protein subunits determine the size and the robustness of the capsid.

It has been previously reported that both hydrophobic interactions and hydrogen bonds play an important role in the recognition of the PDGFR to its ligand [35], Our results show that both of these interactions are important for the binding interaction of PDGF-BB to EGFR. Importantly, both of these interactions are also important in the interaction between EGF and its receptor [1]. It´s important to notice that many tyrosine kinase receptors including PDGFR or EGFR are often able to form heterodimeric Analysis of Binding Residues between PDGF-BB and Epidermal Growth Factor Receptor 37 or hybrid receptors with differential affinity for their ligands [38,39].

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Advances in Computational Biology: Proceedings of the 2nd Colombian Congress on Computational Biology and Bioinformatics (CCBCOL) by Ivan Mura (auth.), Luis F. Castillo, Marco Cristancho, Gustavo Isaza, Andrés Pinzón, Juan Manuel Corchado Rodríguez (eds.)


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