What causes the depolarization of trypsin and trypsinogen fluorescence. Intramolecular mobility or non-radiative energy transfer?

摘要: Analysis of protein data bank information about the coordinates definite atoms macromolecules provides an opportunity to evaluate efficiency non-radiative resonance energy transfer within model fixed, strictly oriented oscillators. Such evaluations for trypsin and trypsinogen (and also complex with a pancreatic inhibitor) show that among each pair tryptophan residues is negligibly small. It shown fairly effective from tyrosine possible. The conclusions have been made Tyr-Trp one factors determining shape polarization spectrum, upon fluorescence excitation at long-wavelength edge absorption depolarization in aqueous solution ambient temperature - compared compounds (tryptophan, N-acetyltryptophan, glycyltryptophan, etc.), under conditions infinite viscosity due Brownian rotational motion as whole well intramolecular mobility. differences level character mobility are discussed.