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dc.contributor.authorJ. Guzmán-Vega, Francisco
dc.contributor.authorT. Arold, Stefan
dc.date.accessioned2020-01-27T08:09:23Z
dc.date.available2020-01-27T08:09:23Z
dc.date.issued2020-1-20
dc.identifier.urihttp://hdl.handle.net/10754/661212
dc.description.abstractUNDERSTANDING GENETIC DISEASE: STRUCTURAL ANALYSIS OF PROTEINS WITH PATIENT-DERIVED MUTATIONS Francisco J. Guzmán-Vega, Stefan T. Arold Abstract Currently, over 8,000 genes have been identified with mutations that are closely associated with human inherited disease. An important application of protein modelling techniques is the analysis of mutated proteins with potential functional or structural alterations that might result in a disease phenotype in humans. We studied and modeled 26 mutations from 15 different proteins related to disease, and classified them by their structural features, which in some cases allow us to predict a mechanism causing the aberrant phenotype. Introduction The most common cause of monogenic disease is a single-base DNA variant resulting in an amino acid substitution, which can affect protein function by different mechanisms: - Folding of the polypeptide chain and stability of the folded conformation - Ligand binding or interaction with binding partners - Posttranslational modifications - Catalytic activity Most common methods to identify and classify non-synonymous mutations with deleterious effects on protein function include: - Using structural information of its three-dimensional environment - Level of conservation and type of residues present at a particular sequence position - Calculation of residue solvent accessibility
dc.relation.urlhttps://epostersonline.com//dh2020/node/70
dc.titleUnderstanding genetic disease: Structural analysis of proteins with patient-derived mutations
dc.typePoster
dc.conference.dateJAN 20 - 22, 2020
dc.conference.nameDigital Health 2020
dc.conference.locationKAUST
dc.contributor.institutionKing Abdullah University of Science and Technology (KAUST), Computational Bioscience Research Center (CBRC), Biological and Environmental Science and Engineering (BESE), Thuwal, 23955-6900, Saudi Arabia
refterms.dateFOA2020-01-27T08:09:23Z


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