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- W2587685943 abstract "Formal assessment of structural similarity is - next to protein structure prediction - arguably the most important unsolved problem in proteomics. In this paper we propose a similarity criterion based on commonalities between the proteins' hydrophobic cores. The hydrophobic core emerges as a result of conformational changes through which each residue reaches its intended position in the protein body. A quantitative criterion based on this phenomenon has been proposed in the framework of the CASP challenge. The structure of the hydrophobic core - including the placement and scope of any deviations from the idealized model - may indirectly point to areas of importance from the point of view of the protein's biological function. Our analysis focuses on an arbitrarily selected target from the CASP11 challenge. The proposed measure, while compliant with CASP criteria (70-80% correlation), involves certain adjustments which acknowledge the presence of factors other than simple spatial arrangement of solids." @default.
- W2587685943 created "2017-02-17" @default.
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- W2587685943 date "2017-02-01" @default.
- W2587685943 modified "2023-10-16" @default.
- W2587685943 title "Determining protein similarity by comparing hydrophobic core structure" @default.
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- W2587685943 doi "https://doi.org/10.1016/j.heliyon.2017.e00235" @default.
- W2587685943 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5300504" @default.
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