NDLI: Thermodynamic stability measurements on multimeric proteins using a new H/D exchange- and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry-based method.

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Thermodynamic stability measurements on multimeric proteins using a new H/D exchange- and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry-based method.

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Thermodynamic stability measurements on multimeric proteins using a new H/D exchange- and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry-based method.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Fitzgerald, Michael C. Wales, Thomas E. Powell, Kendall D.
Description	Country affiliation: United States Author Affiliation: Powell KD ( Department of Chemistry, Duke University, Durham, North Carolina 27708, USA.)
Abstract	We recently reported on a new H/D exchange- and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry-based technique, termed SUPREX, that removes several important limitations associated with measuring the thermodynamic stability of proteins. In contrast to conventional spectroscopy-based techniques for characterizing the equilibrium unfolding behavior of proteins, SUPREX is amenable to the thermodynamic analysis of both purified and unpurified proteins using mg to ng quantities of material. Here we report on the application of SUPREX to the analysis of multimeric protein systems. Included in this work are the SUPREX results we obtained in studies on six model multimeric proteins including the GCN4p1 dimer, the coil-V(a)L(d) trimer, the 4-oxalocrotonate tautomerase (4-OT) hexamer, the Trp repressor (TrpR) dimer, the Arc repressor (ArcR) dimer, and an ArcR mutant (the (DOA20)ArcR) dimer which contained two destabilizing mutations including an Asp to Ala mutation at position 20 and an amide to ester bond mutation between amino acid (aa) residues 19 and 20. As part of the work described here, we present a new method for the analysis of SUPREX data that is generally applicable to both monomeric and multimeric protein systems. Our results on the model proteins in this study indicate that this new method can be used to determine folding free energies for proteins with the accuracy and precision of conventional spectroscopy-based methods.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	4
Volume Number	11
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2002-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Dna-binding Proteins Deuterium Chemistry Hydrogen Isomerases Protein Kinases Repressor Proteins Saccharomyces Cerevisiae Proteins Spectrometry, Mass, Matrix-assisted Laser Desorption-ionization Viral Proteins Enzyme Stability Microchemistry Protein Conformation Protein Folding Sensitivity And Specificity Thermodynamics Viral Regulatory And Accessory Proteins Research Support, U.s. Gov't, Non-p.h.s. Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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