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Titolo:
Measurements of protein stability by H/D exchange and matrix-assisted laser desorption ionization mass spectrometry using picomoles of material
Autore:
Powell, KD; Fitzgerald, MC;
Indirizzi:
Duke Univ, Dept Chem, Durham, NC 27708 USA Duke Univ Durham NC USA 27708Duke Univ, Dept Chem, Durham, NC 27708 USA
Titolo Testata:
ANALYTICAL CHEMISTRY
fascicolo: 14, volume: 73, anno: 2001,
pagine: 3300 - 3304
SICI:
0003-2700(20010715)73:14<3300:MOPSBH>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
RIBONUCLEASE-A; HYDROGEN-EXCHANGE; DENATURATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Fitzgerald, MC Duke Univ, Dept Chem, Durham, NC 27708 USA Duke Univ Durham NC USA 27708 t Chem, Durham, NC 27708 USA
Citazione:
K.D. Powell e M.C. Fitzgerald, "Measurements of protein stability by H/D exchange and matrix-assisted laser desorption ionization mass spectrometry using picomoles of material", ANALYT CHEM, 73(14), 2001, pp. 3300-3304

Abstract

Recently, we reported on a new H/D exchange- and matrix-assisted laser desorption/ionization (MALDI)-based technique, termed SUPREX, that can be usedto measure the thermodynamic stability of a protein (Ghaemmaghami, S.; Fitzgerald, M. C.; Oas, T. G. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 8296-8301), In the work described here, we report on our efforts to optimize the sensitivity of SUPREX analyses. We describe a new sample handling protocol for SUPREX that involves the use of batch chromatography methods with reversed-phase chromatographic media for the microconcentration and desalting of SUPREX samples, Using ribonuclease A as a model protein system, we demonstrate that our new protocol permits the SUPREX analysis of as little as 10 pmol of protein, This amount: of protein is 100-fold less than the amount of material required in our initial SUPREX protocol, and it is 1-2 orders of magnitude less than the amount of material required in conventional spectroscopy-based methods for measuring the thermodynamic stability of a protein.

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Documento generato il 14/07/20 alle ore 12:53:50