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Purification of recombinant proteins by fusion with thermally-responsive polypeptides.

Publication ,  Journal Article
Meyer, DE; Chilkoti, A
Published in: Nat Biotechnol
November 1999

Elastin-like polypeptides (ELPs) undergo a reversible, inverse phase transition. Below their transition temperature (Tt), ELPs are soluble in water, but when the temperature is raised above Tt, phase transition occurs, leading to aggregation of the polypeptide. We demonstrate a method for purification of soluble fusion proteins incorporating an ELP tag. Advantages of this method, termed "inverse transition cycling," include technical simplicity, low cost, ease of scale-up, and capacity for multiplexing. More broadly, the ability to environmentally modulate the physicochemical properties of recombinant proteins by fusion with ELPs will allow diverse applications in bioseparation, immunoassays, biocatalysis, and drug delivery.

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Published In

Nat Biotechnol

DOI

ISSN

1087-0156

Publication Date

November 1999

Volume

17

Issue

11

Start / End Page

1112 / 1115

Location

United States

Related Subject Headings

  • Thioredoxins
  • Recombinant Proteins
  • Peptides
  • Molecular Sequence Data
  • Elastin
  • Base Sequence
  • Amino Acid Sequence
 

Citation

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MLA
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Meyer, D. E., & Chilkoti, A. (1999). Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat Biotechnol, 17(11), 1112–1115. https://doi.org/10.1038/15100
Meyer, D. E., and A. Chilkoti. “Purification of recombinant proteins by fusion with thermally-responsive polypeptides.Nat Biotechnol 17, no. 11 (November 1999): 1112–15. https://doi.org/10.1038/15100.
Meyer DE, Chilkoti A. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat Biotechnol. 1999 Nov;17(11):1112–5.
Meyer, D. E., and A. Chilkoti. “Purification of recombinant proteins by fusion with thermally-responsive polypeptides.Nat Biotechnol, vol. 17, no. 11, Nov. 1999, pp. 1112–15. Pubmed, doi:10.1038/15100.
Meyer DE, Chilkoti A. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat Biotechnol. 1999 Nov;17(11):1112–1115.

Published In

Nat Biotechnol

DOI

ISSN

1087-0156

Publication Date

November 1999

Volume

17

Issue

11

Start / End Page

1112 / 1115

Location

United States

Related Subject Headings

  • Thioredoxins
  • Recombinant Proteins
  • Peptides
  • Molecular Sequence Data
  • Elastin
  • Base Sequence
  • Amino Acid Sequence