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Penn State University


Degree: MS, Chemistry, 2010, Penn State University

The assembly of bacteriophage T4 leading strand polymerase holoenzyme is accomplished with coordination of multi-proteins. To study the stepwise mechanism of this process, single molecule fluorescence resonance energy transfer (smFRET) technique was used. Clamp loading and unloading of T4 were examined by comparing the FRET signal between holoenzyme with and without its polymerase, and by comparing the FRET signal between the hydrolysable holoenzyme and non-hydrolysable holoenzyme. Results showed that the clamp loading is a multi-step mechanism involving various yet unidentified conformations of clamp•clamp-loader complex. It was suggested that there might be three intermediate states of the holoenzyme. The population of the intermediate species and the rate of assembly of the holoenzyme complex from the DNA are greatly enhanced by the presence of the polymerase.

Subjects/Keywords: T4 Clamp; FRET

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APA (6th Edition):

Ren, W. (2010). SINGLE MOLECULE FRET STUDY OF. (Masters Thesis). Penn State University. Retrieved from

Chicago Manual of Style (16th Edition):

Ren, Wenhui. “SINGLE MOLECULE FRET STUDY OF.” 2010. Masters Thesis, Penn State University. Accessed November 14, 2019.

MLA Handbook (7th Edition):

Ren, Wenhui. “SINGLE MOLECULE FRET STUDY OF.” 2010. Web. 14 Nov 2019.


Ren W. SINGLE MOLECULE FRET STUDY OF. [Internet] [Masters thesis]. Penn State University; 2010. [cited 2019 Nov 14]. Available from:

Council of Science Editors:

Ren W. SINGLE MOLECULE FRET STUDY OF. [Masters Thesis]. Penn State University; 2010. Available from: