We present here use of GLGVP for tagging and purifying a gadolinium binding protein domain.https://engagedscholarship.csuohio.edu/u_poster_2012/1027/thumbnail.jp

Mullins, Teisha L.

English

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Cleveland State University
EngagedScholarship@CSU
Undergraduate Research Posters 2012 Undergraduate Research Posters
9-6-2012
Obtaining a Pure Protein Using an ELP-Tagged
TEV Protease
Teisha L. Mullins
Cleveland State University, T.L.MULLINS@csuohio.edu
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Recommended Citation
Mullins, Teisha L., "Obtaining a Pure Protein Using an ELP-Tagged TEV Protease" (2012). Undergraduate Research Posters 2012. 27.
https://engagedscholarship.csuohio.edu/u_poster_2012/27
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Cleveland State University.
Obtaining a Pure Protein Using an ELP-Tagged TEV Protease 
College of Sciences and Health Professions 
 
Student Researcher:  Teisha Mullins 
Faculty Advisors:  Kiril A. Streletzky, Ph.D., Department of Physics; 
Nolan B Holland, Ph.D., Department of Chemical and Biochemical 
Engineering 
Abstract 
Elastin-like polypeptides (ELPs) reversibly aggregate and phase separate above 
and solubilize below a specific transition temperature (Tt). ELPs are composed 
of repeats of the structural sequence of the elastin protein, Gly-Xaa-Gly-Val-Pro 
(GXGVP)n. Xaa is a “guest residue” in the sequence and can be any amino acid, 
with the exception of proline, P, in order to alter the temperature response. ELPs 
can then be attached to recombinant target proteins as a tag to facilitate protein 
purification. 
 
We present here use of GLGVP for tagging and purifying a gadolinium binding 
protein domain. Leucine is used as the guest residue in order to lower the Tt 
below room temperature, enabling purification to take place over a more 
manageable temperature range. After protein purification, it is ideal to remove 
the ELP tag from the target protein. To accomplish this, a tobacco etch virus 
(TEV) protease cleavage site was inserted between the target protein and the 
ELP tag. The TEV protease is also tagged with an ELP so that after proteolytic 
cleavage the ELP tag from the target protein, a single round of thermal cycling 
can remove both the free ELP tag and the ELP-tagged TEV protease, leaving the 
purified target protein. 
 
  


Obtaining a Pure Protein Using an ELP-Tagged TEV Protease

https://engagedscholarship.csuohio.edu/cgi/viewcontent.cgi?article=1027&amp;context=u_poster_2012

Obtaining a Pure Protein Using an ELP-Tagged TEV Protease

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