The conformational polymorphism of the green fluorescent protein |
| |
Authors: | Haidong Tan Yueguang Li Ling Chen Takayuki Kudoh Tomonari Kasai Masaharu Seno |
| |
Affiliation: | 1.Dalian Institute of Chemical Physics,CAS,Dalian,China;2.Department of General Surgery,Tianjin 4th Centre Hospital,Zhongshanlu, Hebeiqu, Tianjin,People’s Republic of China;3.Department of Medical and Bioengineering Science, Graduate School of Natural Science and Technology,Okayama University,Okayama,Japan |
| |
Abstract: | Green fluorescent protein (GFPuv) has been widely used as a reporter fused to individual targeting sequences. However, its state in liquid and its effect on other proteins are still unclear. The conformational polymorphisms of glutathione-S-transferase-green fluorescent protein (GST-GFPuv), GFPuv and GST were analyzed by native polyacrylamide gel, indicating that GST was in many different states while GFPuv and GST-GFPuv were only in four and two slightly different states. Four different circular dichroism spectra were obtained from the GFPuv polymorphisms. The single molecular behavior of GST-GFPuv and GFPuv was also characterized by MALDI-TOF MS. Thus, we demonstrated that: (1) there might be four different structural polymorphisms for the native GFPuv; (2) GFPuv could reduce its partner’s polymorphism as a fusion protein. Although GFPuv had many merits as a reporter, its unreliability was found in the study. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|