Chiral Ramachandran Plots II: General Trends and Protein Chirality Spectra

Huan Wang, David Avnir, Inbal Tuvi-Arad

פרסום מחקרי: פרסום בכתב עתמאמרביקורת עמיתים


The degree of chirality of protein backbone residues is used to enrich the Ramachandran plot (RP) and create three-dimensional chiral RPs with much more structural information. Detailed comparative analysis of the four classical RPs (general, glycine, proline, and pre-proline) is provided, including statistical analysis of quantitative chirality distributions in the maps and in the secondary structures. Our results show that points with outlier chirality levels represent special transitional points in the folded protein such as α-helix kinks, twists of β-strands, and transition points between secondary structures. A protein chirality spectrum in which the degree of chirality of each residue is plotted against the sequence number explores these special points. More than 65000 residues extracted from 200 high-quality proteins are used for this study, which shows that quantitative chirality is a general and useful structural parameter for protein conformational studies.

שפה מקוריתאנגלית
עמודים (מ-עד)6395-6403
מספר עמודים9
כתב עתBiochemistry
מספר גיליון45
מזהי עצם דיגיטלי (DOIs)
סטטוס פרסוםפורסם - 13 נוב׳ 2018

הערה ביבליוגרפית

Publisher Copyright:
© 2018 American Chemical Society.

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