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• W3011246329 abstract "Protein structures, usually visualized in various highly idealized forms focusing on the three-dimensional arrangements of secondary structure elements, can also be described as lists of interacting residues or atoms and visualized as two-dimensional distance or contact maps. We show that contact maps provide an ideal tool to describe and analyze differences between structures of proteins in different conformations. Expanding functionality of the PDBFlex server and database developed previously in our group, we describe how analysis of difference contact maps (DCMs) can be used to identify critical interactions stabilizing alternative protein conformations, recognize residues and positions controlling protein functions and build hypotheses as to molecular mechanisms of disease mutations." @default.
• W3011246329 created "2020-03-23" @default.
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• W3011246329 date "2020-03-12" @default.
• W3011246329 modified "2023-10-14" @default.
• W3011246329 title "Difference contact maps: From what to why in the analysis of the conformational flexibility of proteins" @default.
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• W3011246329 doi "https://doi.org/10.1371/journal.pone.0226702" @default.
• W3011246329 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7067477" @default.
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