Pyrene: A Probe to Study Protein Conformation and Conformational Changes

被引:235
|
作者
Bains, Gursharan [1 ]
Patel, Arti B. [1 ]
Narayanaswami, Vasanthy [1 ,2 ]
机构
[1] Calif State Univ Long Beach, Dept Chem & Biochem, Long Beach, CA 90840 USA
[2] Childrens Hosp Oakland Res Inst, Oakland, CA 94609 USA
来源
MOLECULES | 2011年 / 16卷 / 09期
关键词
pyrene; excimer; monomer; Py value; apolipoproteins; fluorescence; protein oligomerization; protein-lipid interactions; protein-membrane interactions; HUMAN APOLIPOPROTEIN-E; VIBRONIC BAND INTENSITIES; GLUTATHIONE-S-TRANSFERASE; LOW-DENSITY-LIPOPROTEIN; CARBONIC ANHYDRASE-II; CARDIAC TROPONIN-C; EXCIMER FLUORESCENCE; APOLIPOPHORIN-III; LABELED TROPOMYOSIN; SKELETAL-MUSCLE;
D O I
10.3390/molecules16097909
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The review focuses on the unique spectral features of pyrene that can be utilized to investigate protein structure and conformation. Pyrene is a fluorescent probe that can be attached covalently to protein side chains, such as sulfhydryl groups. The spectral features of pyrene are exquisitely sensitive to the microenvironment of the probe: it exhibits an ensemble of monomer fluorescence emission peaks that report on the polarity of the probe microenvironment, and an additional band at longer wavelengths, the appearance of which reflects the presence of another pyrene molecule in spatial proximity(similar to 10 angstrom). Its high extinction coefficient allows us to study labeled proteins in solution at physiologically relevant concentrations. The environmentally-and spatially-sensitive features of pyrene allow monitoring protein conformation, conformational changes, protein folding and unfolding, protein-protein, protein-lipid and protein-membrane interactions.
引用
收藏
页码:7909 / 7935
页数:27
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