Role of Interfacial Viscosity and pH in L-Phenylalanine, L-Tryptophan Molecular Rotors

Protein folding involves the aminoacid sequence to come forth and form an energy minimized structure. Recently molecular crowding leading to increase in viscosity is said to be one of the major concerns affecting protein folding. Many external fluorescent probes are used to detect such increases in viscosity. Since most of the protein sequences contain L-Phe and L-Trp, in this study we have used these aminoacids as probes to detect changes in viscosity. This study will help to advance the knowledge on molecular crowding effects in protein folding.