ArticleJournal of the American Society for Mass Spectrometry2009
HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1.
Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Examining DNA Structures with In-droplet Hydrogen/Deuterium Exchange Mass Spectrometry.International journal of mass spectrometry · 2024Article
- Parallel Chemoselective Profiling for Mapping Protein Structure.Cell chemical biology · 2020Article
- Collagen I Weakly Interacts with the β-Sheets of βJournal of the American Chemical Society · 2020Article
- Fast photochemical oxidation of proteins (FPOP): A powerful mass spectrometry-based structural proteomics tool.The Journal of biological chemistry · 2019Review
- Comparing Hydrogen Deuterium Exchange and Fast Photochemical Oxidation of Proteins: a Structural Characterisation of Wild-Type and ΔN6 βJournal of the American Society for Mass Spectrometry · 2018Article
- Direct evidence for conformational dynamics in major histocompatibility complex class I molecules.The Journal of biological chemistry · 2017Article
- Increased β-Sheet Dynamics and D-E Loop Repositioning Are Necessary for Cu(II)-Induced Amyloid Formation by β-2-Microglobulin.Biochemistry · 2017Article
- Stepwise unfolding of human βEuropean biophysics journal : EBJ · 2017Article
- Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly.Molecular cell · 2014Article
- Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Journal of the American Chemical Society · 2014Article
- Insights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometry.Molecular bioSystems · 2014Article
- NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.Journal of biomolecular NMR · 2013Article
- The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH.Rapid communications in mass spectrometry : RCM · 2012Article
- Understanding the complex mechanisms of β2-microglobulin amyloid assembly.The FEBS journal · 2011Review
- Disulfide bonds in ER protein folding and homeostasis.Current opinion in cell biology · 2011Review
- Determining the topology of virus assembly intermediates using ion mobility spectrometry-mass spectrometry.Rapid communications in mass spectrometry : RCM · 2010Article
- Mass spectrometry and the amyloid problem--how far can we go in the gas phase?Journal of the American Society for Mass Spectrometry · 2010Article
- DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded form.Protein science : a publication of the Protein Society · 2010Article
- Hydrogen exchange mass spectrometry: what is it and what can it tell us?Analytical and bioanalytical chemistry · 2010Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The light chain of the major histocompatibility complex class 1 (MHC-1), the protein beta(2)-microglobulin (beta(2)m), has amyloidogenic properties that arise only upon its dissociation from the MHC-1. Here hydrogen/deuterium exchange electrospray ionization mass spectrometry (HDX-ESI-MS) has been used to compare the solution dynamics of beta(2)m in its MHC-1 bound state compared with those of beta(2)m as a free monomer. The capability of tandem mass spectrometry to dissociate the MHC-1 into its individual constituents in the gas phase following deuterium incorporation in solution has permitted the direct observation of the exchange properties of MHC-1 bound beta(2)m for the first time. The HDX-ESI-MS data show clearly that the H-->D exchange of MHC-1 bound beta(2)m follows EX2 kinetics and that about 20 protons remain protected from exchange after 17 days. Free from the MHC-1, monomeric beta(2)m exhibits significantly different HDX behavior, which encompasses both EX1 and EX2 kinetics. The EX2 kinetics indicate a tenfold increase in the rate of exchange compared with MHC-1 bound beta(2)m, with just 10 protons remaining protected from EX2 exchange and therefore exchanging only via the EX1 mechanism. The EX1 kinetics observed for unbound beta(2)m are consistent with unfolding of its exchange-protected core with a t(1/2) of 68 min (pH 7, 37 degrees C). Thus, upon dissociation from the stabilizing influence of the MHC-1, free beta(2)m becomes highly dynamic and undergoes unfolding transitions that result in an aggregation-competent protein.
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