Evaluation of variability in high-resolution protein structures by global distance scoring.

ABSTRACT: Systematic analysis of the statistical and dynamical properties of proteins is critical to understanding cellular events. Extraction of biologically relevant information from a set of high-resolution structures is important because it can provide mechanistic details behind the functional properties of protein families, enabling rational comparison between families. Most of the current structural comparisons are pairwise-based, which hampers the global analysis of increasing contents in the Protein Data Bank. Additionally, pairing of protein structures introduces uncertainty with respect to reproducibility because it frequently accompanies other settings for superimposition. This study introduces intramolecular distance scoring for the global analysis of proteins, for each of which at least

SUBMITTER: Anzai R 

PROVIDER: S-EPMC5857612 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature