title: Study protein folding and aggregation using nonnatural amino acid p-cyanophenylalanine as a sensitive optical probe.
abstract: Incorporation of nonnatural amino acids with a variety of special side groups into protein sequences has substantially expanded the experimental means of exploring protein structures and functions. Recently, p-cyanophenylalanine (PheCN), the nitrile analogue of phenylalanine, has been used as a novel optical probe for protein binding and folding studies. The fluorescence emission of PheCN is sensitive to solvent and local environment of the residue, making it a useful fluorescent probe of protein structural change at residue-specific resolution. Moreover, the utility of PheCN is increased by its ability to excite tryptophan fluorescence via the mechanism of fluorescence resonance energy transfer. PheCN could be applied to study a variety of biological problems, e.g., protein folding/unfolding and protein aggregation.
authors.affiliation: Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL, USA.
authors.forename: Deguo
authors.initials: D
authors.lastname: Du
authors.forename: Haiyang
authors.initials: H
authors.lastname: Liu
authors.forename: Bimlesh
authors.initials: B
authors.lastname: Ojha
mesh_terms: D000409:Alanine / Q000031:analogs & derivatives* / Q000737:chemistry; D000596:Amino Acids / Q000737:chemistry*; D016229:Amyloid beta-Peptides / Q000737:chemistry; D007700:Kinetics; D009570:Nitriles / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000302:isolation & purification; D011485:Protein Binding; D017510:Protein Folding; D013050:Spectrometry, Fluorescence / Q000379:methods; D010649:Phenylalanine / Q000031:analogs & derivatives
chemical_list: D000409:Alanine; D000596:Amino Acids; D016229:Amyloid beta-Peptides; D009570:Nitriles; D010455:Peptides; C530634:p-cyanophenylalanine; D010649:Phenylalanine