A database of calculated solution parameters for the AlphaFold predicted protein structures.

ABSTRACT: Recent spectacular advances by AI programs in 3D structure predictions from protein sequences have revolutionized the field in terms of accuracy and speed. The resulting "folding frenzy" has already produced predicted protein structure databases for the entire human and other organisms' proteomes. However, rapidly ascertaining a predicted structure's reliability based on measured properties in solution should be considered. Shape-sensitive hydrodynamic parameters such as the diffusion and sedimentation coefficients ([Formula: see text], [Formula: see text]) and the intrinsic viscosity ([η]) can provide a rapid assessment of the overall structure likeliness, and SAXS would yield the structure-related pair-wise distance distribution function p(r) vs. r. Using the extensively validated UltraS

SUBMITTER: Brookes E 

PROVIDER: S-EPMC9072687 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature