The fluorescence properties of tryptophan and tryptophan-retinal Schiff base are investigated in a reverse micellar matrix of sodium bis(2-ethylhexyl) sulphosuccinate, a membrane mimetic system. The results are discussed in terms of energy transfer interaction between retinal and tryptophan in the native protein and the conformational aspects of tryptophan residues in the protein
The fluorescence resonance energy transfer (FRET) from tryptophan (Trp) to folic acid (FA) in aqueou...
The presence of tryptophan residues as intrinsic fluorophores in most proteins makes them an obvious...
The comparison between UV transient absorption spectra of wild type bacteriorhodopsin and two trypto...
All-trans-N-retinylidenetryptamine Schiff base was incorporated into aerosol-OT (AOT, sodium bis(2-e...
Two new long chain tryptophan compounds viz [3-(indolyl-3′)-2-(N-octadecamido)]-methylpropionate (4)...
The Schiff bases of retinal with natural amino acids can conveniently be prepared in sodium bis(2-et...
Many peptides containing tryptophan have therapeutic uses and can be studied by their fluorescent pr...
The fluorescence properties of indole derivatives, lysozyme and azurin were investigated in reverse ...
The fluorescence and circular dichroism of proteins in reverse micelles: application to the photophy...
The tryptophan fluorescence of proteins has been widely used to examine protein structure, ligand bi...
The intrinsic fluorescent amino acid tryptophan is the unanimous choice for the spectroscopic invest...
The fluorescence of a membrane-bound tryptophan derivative (tryptophan octyl ester, TOE) has been ex...
Many peptides containing tryptophan have therapeutic uses and can be studied by their fluorescent pr...
The fluorescence of all-trans-N-retinylidenetryptamine (1) in AOT solubilized water pool in n-heptan...
F resonance energy transfer (FRET) occurs when the distance between a donor fluorophore and an accep...
The fluorescence resonance energy transfer (FRET) from tryptophan (Trp) to folic acid (FA) in aqueou...
The presence of tryptophan residues as intrinsic fluorophores in most proteins makes them an obvious...
The comparison between UV transient absorption spectra of wild type bacteriorhodopsin and two trypto...
All-trans-N-retinylidenetryptamine Schiff base was incorporated into aerosol-OT (AOT, sodium bis(2-e...
Two new long chain tryptophan compounds viz [3-(indolyl-3′)-2-(N-octadecamido)]-methylpropionate (4)...
The Schiff bases of retinal with natural amino acids can conveniently be prepared in sodium bis(2-et...
Many peptides containing tryptophan have therapeutic uses and can be studied by their fluorescent pr...
The fluorescence properties of indole derivatives, lysozyme and azurin were investigated in reverse ...
The fluorescence and circular dichroism of proteins in reverse micelles: application to the photophy...
The tryptophan fluorescence of proteins has been widely used to examine protein structure, ligand bi...
The intrinsic fluorescent amino acid tryptophan is the unanimous choice for the spectroscopic invest...
The fluorescence of a membrane-bound tryptophan derivative (tryptophan octyl ester, TOE) has been ex...
Many peptides containing tryptophan have therapeutic uses and can be studied by their fluorescent pr...
The fluorescence of all-trans-N-retinylidenetryptamine (1) in AOT solubilized water pool in n-heptan...
F resonance energy transfer (FRET) occurs when the distance between a donor fluorophore and an accep...
The fluorescence resonance energy transfer (FRET) from tryptophan (Trp) to folic acid (FA) in aqueou...
The presence of tryptophan residues as intrinsic fluorophores in most proteins makes them an obvious...
The comparison between UV transient absorption spectra of wild type bacteriorhodopsin and two trypto...