An Improved Diabatization Scheme for Computing the Electronic Circular Dichroism of Proteins.

ABSTRACT: We advance the quality of first-principles calculations of protein electronic circular dichroism (CD) through an amelioration of a key deficiency of a previous procedure that involved diabatization of electronic states on the amide chromophore (to obtain interamide couplings) in a β-strand conformation of a diamide. This yields substantially improved calculated far-ultraviolet (far-UV) electronic circular dichroism (CD) spectra for β-sheet conformations. The interamide couplings from the diabatization procedure for 13 secondary structural elements (13 diamide structures) are applied to compute the CD spectra for seven example proteins: myoglobin (α helix), jacalin (β strand), concanavalin A (β type I), elastase (β type II), papain (α + β), 3₁₀-helix bundle (3₁₀-helix)

SUBMITTER: Rogers DM 

PROVIDER: S-EPMC11301672 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature