Variation of intrinsic tryptophan (Trp) fluorescence intensity and lifetime in proteins is widely
exploited to follow changes in protein structure such as folding/unfolding, substrate or ligand …

This work reports an explanation for the unusual monoexponential fluorescence decay of 5-
fluorotryptophan (5FTrp) in single-Trp mutant proteins [Broos, J.; Maddalena, F.; Hesp, BHJ …

The peptide bond quenches tryptophan fluorescence by excited-state electron transfer,
which probably accounts for most of the variation in fluorescence intensity of peptides and …

The wavelength of maximum emission of tryptophan depends on the local electrostatic
environment of the indole chromophore. The time-resolved emission spectra of seven rigid …

Human serum albumin (HSA) plays important roles in transport of fatty acids and binding a
variety of drugs and organic compounds in the circulatory system. This protein experiences …

Mutagenesis studies on the phototropin‐related protein YtvA from Bacillus subtilis have
revealed the role of selected structural elements in interdomain communication. The LOV …

Abstract Structure of immobilised enzymes: Circular dichroism, infrared and fluorescence
spectroscopic methods are used to characterise in situ structural stability of enzymes …

The integral membrane protein M2 of influenza A virus assembles as a tetrameric bundle to
form a proton-conducting channel that is activated by low pH. The side chain of His37 in the …

The synthetic cyclic octapeptide octreotide is less stable under UV and fluorescent lights
than its naturally occurring derivative somatostatin. Upon irradiation at λ> 290 nm, and in the …

The temperature dependence of tryptophan fluorescence lifetime in an aqueous solution,
aqueous solutions of glycerol (50 and 75%, v/v) and dimethyl sulfoxide (DMSO)(50 and …