Factors correlating with significant differences between X-ray structures of myoglobin.

ABSTRACT: Validation of general ideas about the origins of conformational differences in proteins is critical in order to arrive at meaningful functional insights. Here, principal component analysis (PCA) and distance difference matrices are used to validate some such ideas about the conformational differences between 291 myoglobin structures from sperm whale, horse and pig. Almost all of the horse and pig structures form compact PCA clusters with only minor coordinate differences and outliers that are easily explained. The 222 whale structures form a few dense clusters with multiple outliers. A few whale outliers with a prominent distortion of the GH loop are very similar to the cluster of horse structures, which all have a similar GH-loop distortion apparently owing to intermolecular crystal latti

SUBMITTER: Rashin AA 

PROVIDER: S-EPMC3940193 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature