Du Deguo, Liu Haiyang, Ojha Bimlesh
Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL, USA.
Methods Mol Biol. 2013;1081:77-89. doi: 10.1007/978-1-62703-652-8_6.
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.
将带有各种特殊侧链基团的非天然氨基酸掺入蛋白质序列中，极大地扩展了探索蛋白质结构和功能的实验手段。最近，对氰基苯丙氨酸（PheCN），苯丙氨酸的腈类似物，已被用作蛋白质结合和折叠研究的新型光学探针。PheCN的荧光发射对残基的溶剂和局部环境敏感，使其成为在残基特异性分辨率下蛋白质结构变化的有用荧光探针。此外，PheCN通过荧光共振能量转移机制激发色氨酸荧光的能力增加了其效用。PheCN可用于研究各种生物学问题，例如蛋白质折叠/去折叠和蛋白质聚集。
