Folding kinetics of the S100A11 protein dimer studied by time-resolved electrospray mass spectrometry and pulsed hydrogen-deuterium exchange

Biochemistry
Jingxi PanL Konermann

Abstract

This study reports the application of electrospray ionization (ESI) mass spectrometry (MS) with on-line rapid mixing for millisecond time-resolved studies of the refolding and assembly of a dimeric protein complex. Acid denaturation of S100A11 disrupts the native homodimeric protein structure. Circular dichroism and HSQC nuclear magnetic resonance measurements reveal that the monomeric subunits unfold to a moderate degree but retain a significant helicity and some tertiary structural elements. Following a rapid change in solution conditions to a slightly basic pH, the native protein reassembles with an effective rate constant of 6 s(-)(1). The ESI charge state distributions measured during the reaction suggest the presence of three kinetic species, namely, a relatively unfolded monomer (M(U)), a more tightly folded monomeric reaction intermediate (M(F)), and dimeric S100A11. These three forms exhibit distinct calcium binding properties, with very low metal loading levels for M(U), up to two calcium ions for M(F), and up to four for the dimer. Surprisingly, on-line pulsed hydrogen-deuterium exchange (HDX) reveals that each of the monomeric forms of the protein comprises two subspecies that can be distinguished on the basis of th...Continue Reading

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Citations

Dec 19, 2012·Journal of the American Society for Mass Spectrometry·Lu DengJohn S Klassen
Sep 19, 2006·Journal of the American Society for Mass Spectrometry·Brian L Boys, Lars Konermann
Oct 11, 2008·Journal of the American Society for Mass Spectrometry·Tamanna Rob, Derek J Wilson
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Oct 22, 2010·BMC Bioinformatics·Ugur UzunerJoshua S Yuan
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Aug 13, 2009·Mass Spectrometry Reviews·Lars KonermannXin Tong
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Aug 19, 2008·Journal of Molecular Biology·Gary S ShawStephen P Bottomley
May 30, 2012·European Journal of Mass Spectrometry·Tamanna Rob, Derek J Wilson
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