Study of Organization and Dynamics of Multi-Tryptophan Protein Molecules Utilizing Red Edge Excitation Shift Approach: A Review

Anisur R. Molla1,*, and Pritha Mandal2,

1Department of Chemistry, Bidhannagar College, Salt Lake, Kolkata-700064, India

2Department of Chemistry, Krishnagar Government College, Krishnagar-741101, India

*Corresponding author: E-mail: anisur.chem@gmail.com

Abstract

A shift in the fluorescence emission maxima with gradual increase in excitation wavelength is termed as red edge excitation shift (REES). Tryptophan residues are widely utilized as intrinsic fluorescence probe to investigate the protein structures. Wavelength selective tryptophan fluorescence can explore the dynamics of surrounded water molecules, the ubiquitous biological solvent. Thus REES experiment of various protein conformational states can provide significant input to the study of protein folding pathway and it can also be useful to study interaction of proteins with others. In this review article, we shall focus on red edge effect of various multi-tryptophan proteins in their respective native, intermediate and denatured state.

Keywords

Fluorescence, Multi-tryptophan protein, Red edge excitation shift, Red edge effect, Protein structure.

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