We present a coarse residue-based computational method to rapidly compute the
solution scattering profile from a protein with dynamical fluctuations. The method is built upon a
coarse-grained (CG) representation of the protein. This CG representation takes advantage of the intrinsic low-resolution and CG nature of
solution scattering data. It allows rapid
scattering determination from a large number of conformations that can be extracted from CG simulations to obtain
scattering characterization of
protein conformations. The method includes several important elements, effective residue structure factors
derived from the
Protein Data Bank, explicit treatment of
water molecules in the hydration layer at the surface of the protein, and an
ensemble average of
scattering from a variety of appropriate conformations to account for
macromolecular flexibility. This simplified method is calibrated and illustrated to accurately reproduce the experimental
scattering curve of Hen
egg white lysozyme. We then illustrated the applications of this
CG method by computing the
solution scattering patterns of several representative protein folds and multiple conformational states. The results suggest that
solution scattering data, when combined with the reliable computational method that we developed, show great potential for a better structural description of multidomain complexes in different functional states, and for recognizing structural folds when
sequence similarity to a protein of known structure is low.
