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• W1993402893 abstract "The cores of globular proteins are densely packed, resulting in complicated networks of structural interactions. These interactions in turn give rise to dynamic structural correlations over a wide range of time scales. Accurate analysis of these complex correlations is crucial for understanding biomolecular mechanisms and for relating structure to function. Here we report a highly accurate technique for inferring the major modes of structural correlation in macromolecules using likelihood-based statistical analysis of sets of structures. This method is generally applicable to any ensemble of related molecules, including families of nuclear magnetic resonance (NMR) models, different crystal forms of a protein, and structural alignments of homologous proteins, as well as molecular dynamics trajectories. Dominant modes of structural correlation are determined using principal components analysis (PCA) of the maximum likelihood estimate of the correlation matrix. The correlations we identify are inherently independent of the statistical uncertainty and dynamic heterogeneity associated with the structural coordinates. We additionally present an easily interpretable method (PCA plots) for displaying these positional correlations by color-coding them onto a macromolecular structure. Maximum likelihood PCA of structural superpositions, and the structural PCA plots that illustrate the results, will facilitate the accurate determination of dynamic structural correlations analyzed in diverse fields of structural biology." @default.
• W1993402893 created "2016-06-24" @default.
• W1993402893 creator A5031343617 @default.
• W1993402893 creator A5046700536 @default.
• W1993402893 date "2008-02-15" @default.
• W1993402893 modified "2023-09-28" @default.
• W1993402893 title "Accurate Structural Correlations from Maximum Likelihood Superpositions" @default.
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• W1993402893 doi "https://doi.org/10.1371/journal.pcbi.0040043" @default.
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