The conformational polymorphism of the green fluorescent protein.

Haidong Tan, Yueguang Li, Ling Chen, Takayuki Kudoh, Tomonari Kasai, Masaharu Seno

Research output: Contribution to journalArticle

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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.

Original languageEnglish
Pages (from-to)156-161
Number of pages6
JournalMolekuliarnaia biologiia
Volume46
Issue number1
Publication statusPublished - Jan 1 2012

ASJC Scopus subject areas

  • Medicine(all)

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