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A quantitative, high-throughput screen for protein stability.

Publication ,  Journal Article
Ghaemmaghami, S; Fitzgerald, MC; Oas, TG
Published in: Proc Natl Acad Sci U S A
July 18, 2000

In proteomic research, it is often necessary to screen a large number of polypeptides for the presence of stable structure. Described here is a technique (referred to as SUPREX, stability of unpurified proteins from rates of H/D exchange) for measuring the stability of proteins in a rapid, high-throughput fashion. The method uses hydrogen exchange to estimate the stability of microgram quantities of unpurified protein extracts by using matrix-assisted laser desorption/ionization MS. The stabilities of maltose binding protein and monomeric lambda repressor variants determined by SUPREX agree well with stability data obtained from conventional CD denaturation of purified protein. The method also can detect the change in stability caused by the binding of maltose to maltose binding protein. The results demonstrate the precision of the method over a wide range of stabilities.

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Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

July 18, 2000

Volume

97

Issue

15

Start / End Page

8296 / 8301

Location

United States

Related Subject Headings

  • Viral Regulatory and Accessory Proteins
  • Viral Proteins
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Repressor Proteins
  • Recombinant Fusion Proteins
  • Maltose-Binding Proteins
  • Maltose
  • DNA-Binding Proteins
  • Carrier Proteins
  • Bacteriophage lambda
 

Citation

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Ghaemmaghami, S., Fitzgerald, M. C., & Oas, T. G. (2000). A quantitative, high-throughput screen for protein stability. Proc Natl Acad Sci U S A, 97(15), 8296–8301. https://doi.org/10.1073/pnas.140111397
Ghaemmaghami, S., M. C. Fitzgerald, and T. G. Oas. “A quantitative, high-throughput screen for protein stability.Proc Natl Acad Sci U S A 97, no. 15 (July 18, 2000): 8296–8301. https://doi.org/10.1073/pnas.140111397.
Ghaemmaghami S, Fitzgerald MC, Oas TG. A quantitative, high-throughput screen for protein stability. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8296–301.
Ghaemmaghami, S., et al. “A quantitative, high-throughput screen for protein stability.Proc Natl Acad Sci U S A, vol. 97, no. 15, July 2000, pp. 8296–301. Pubmed, doi:10.1073/pnas.140111397.
Ghaemmaghami S, Fitzgerald MC, Oas TG. A quantitative, high-throughput screen for protein stability. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8296–8301.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

July 18, 2000

Volume

97

Issue

15

Start / End Page

8296 / 8301

Location

United States

Related Subject Headings

  • Viral Regulatory and Accessory Proteins
  • Viral Proteins
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Repressor Proteins
  • Recombinant Fusion Proteins
  • Maltose-Binding Proteins
  • Maltose
  • DNA-Binding Proteins
  • Carrier Proteins
  • Bacteriophage lambda