title: Modeling the absorption spectrum of tryptophan in proteins.
abstract: We have applied time-dependent density functional theory (TDDFT) to study the valence pi-pi* excited states of the tryptophan chromophore in the environment of the proteins barnase and human serum albumin. The chromophore is represented by indole. Due to the approximate nature of TDDFT, in the gas phase the calculated vertical transition energies to the 1L valence states are reordered with respect to experiment. The 1L(a) state responds more than the 1L(b) state to the local environment, described fully at the TDDFT level, and to bulk environment, described by a set of point charges. Nevertheless, the vertical transitions are readily identified. For human serum albumin, our calculations predict distinct spectral characteristics between structures with different tryptophan side chain torsion angles. The computational tractability of TDDFT relative to more accurate ab initio methods allows a large part of the surrounding protein environment (up to 100 atoms) to be explicitly included in the TDDFT calculations.
authors.affiliation: School of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, United Kingdom.
authors.forename: David M
authors.initials: DM
authors.lastname: Rogers
authors.forename: Nicholas A
authors.initials: NA
authors.lastname: Besley
authors.forename: Paul
authors.initials: P
authors.lastname: O'Shea
authors.forename: Jonathan D
authors.initials: JD
authors.lastname: Hirst
mesh_terms: D001407:Bacillus / Q000201:enzymology; D001426:Bacterial Proteins; D006801:Humans; D008956:Models, Chemical; D008958:Models, Molecular; D012260:Ribonucleases / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry*; D013053:Spectrophotometry; D014364:Tryptophan / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D012709:Serum Albumin; D014364:Tryptophan; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease