Electronic trasitions in molecules in static external fields. I. Indole and Trp-59 in ribonuclease T1

P. Ilich, P. H. Axelsen, F. G. Prendergast

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Electronic transition properties of indole perturbed by its environment were calculated by use of quantum-mechanical semi-empirical numerical methods. The environment was represented by a discrete set of charges placed at different positions around the indole ring. Wavelength shifts and transition intensity changes in indole were evaluated for several, specifically modeled geometries of external charges. This methodology was employed to estimate the extent of spectroscopic changes induced by small nonprotein polar species on the Trp-59 residue in the anisotropic environment of the protein ribonuclease T1. The geometry of the residue environment was obtained from dynamically equilibrated X-ray crystallographic data of the protein.

Original languageEnglish (US)
Pages (from-to)341-349
Number of pages9
JournalBiophysical Chemistry
Volume29
Issue number3
DOIs
StatePublished - 1988

Fingerprint

Ribonuclease T1
indoles
Molecules
electronics
molecules
Geometry
proteins
Numerical methods
Proteins
geometry
X rays
Wavelength
X-Rays
methodology
indole
rings
shift
estimates
wavelengths
x rays

Keywords

  • Electronic transition
  • Quantum-mechanical calculation
  • Ribonuclease T
  • Tryptophan

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Physical and Theoretical Chemistry

Cite this

Electronic trasitions in molecules in static external fields. I. Indole and Trp-59 in ribonuclease T1 . / Ilich, P.; Axelsen, P. H.; Prendergast, F. G.

In: Biophysical Chemistry, Vol. 29, No. 3, 1988, p. 341-349.

Research output: Contribution to journalArticle

Ilich, P. ; Axelsen, P. H. ; Prendergast, F. G. / Electronic trasitions in molecules in static external fields. I. Indole and Trp-59 in ribonuclease T1 In: Biophysical Chemistry. 1988 ; Vol. 29, No. 3. pp. 341-349.
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