First-Principles Calculations of Protein Circular Dichroism in the Near Ultraviolet†

摘要: Electronic transitions in aromatic side chains are responsible for the characteristics of proteins near UV. We present first systematic study a large number focused on accurate calculation near-UV circular dichroism (CD) spectra. report new parameter sets derived from ab initio calculations benzene, phenol, and indole that describe valence electronic to (1)L(b), (1)L(a), (1)B(b), (1)B(a) states amino acids phenylalanine, tyrosine, tryptophan. CD spectra were calculated, using matrix method with side-chain parameters, 30 whose crystal structures have been made publicly available. The fully self-consistent yield better than those obtained previous sets. mean absolute errors computed wild-type UV reduced by factor approximately 2. A similiar reduction is found (and difference spectra) mutants involving acids. Empirical modifications model vibronic coupling chromophore phenylalanine offer no overall improvement. Protein principles coupled atomic-level modeling enhance utility interpretability measurements