Author(s)

Vishvanath Tiwari^*, Monalisa Tiwari

Department of Biochemistry, Central University of Rajasthan, Ajmer, India.

Intrinsic fluorescence of tryptophan is a powerful tool that is used to investigate structure, dynamics, and folding-unfolding of proteins. Here, we have signified the importance of selective monitoring of “surface” tryptophans from the “buried” tryptophans in a protein via selective excitation of surface tryptophan using light of 305 nm wavelength. We have also enlightened the effect of pH and temperature on the conformation of protein by selective excitation of surface tryptophan of protein using 305 nm light. The result concludes that this novel approach could be used to investigate surface tryptophan of protein selectively at diverse conditions.

Protein Fluorescence, Tryptophan Fluorescence, Fluorescence Spectroscopy

Tiwari, V. and Tiwari, M. (2015) Investigation of Surface Tryptophan of Protein by Selective Excitation at 305 nm. Journal of Biophysical Chemistry, 6, 87-90. doi: 10.4236/jbpc.2015.63009.