ArticleJournal of the American Society for Mass Spectrometry2013
Time window expansion for HDX analysis of an intrinsically disordered protein.
Article in Journal of the American Society for Mass Spectrometry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
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- Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B.Molecular cell · 2024Article
- Fundamentals of HDX-MS.Essays in biochemistry · 2023Review
- Biophysical and Integrative Characterization of Protein Intrinsic Disorder as a Prime Target for Drug Discovery.Biomolecules · 2023Review
- A neutralizing epitope on the SD1 domain of SARS-CoV-2 spike targeted following infection and vaccination.Cell reports · 2022Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Crystal Structure of the Epo1-Bem3 Complex for Bud Growth.International journal of molecular sciences · 2021Article
- Structural Proteomics Methods to Interrogate the Conformations and Dynamics of Intrinsically Disordered Proteins.Frontiers in chemistry · 2021Review
- HaDeX: an R package and web-server for analysis of data from hydrogen-deuterium exchange mass spectrometry experiments.Bioinformatics (Oxford, England) · 2020Article
- Imidazolium Compounds as Internal Exchange Reporters for Hydrogen/Deuterium Exchange by Mass Spectrometry.Analytical chemistry · 2020Article
- Bridging protein structure, dynamics, and function using hydrogen/deuterium-exchange mass spectrometry.Protein science : a publication of the Protein Society · 2020Review
- Dynamics and Location of the Allosteric Midazolam Site in Cytochrome P4503A4 in Lipid Nanodiscs.Biochemistry · 2020Article
- The Order-Disorder Continuum: Linking Predictions of Protein Structure and Disorder through Molecular Simulation.Scientific reports · 2020Review
- Tracking Higher Order Protein Structure by Hydrogen-Deuterium Exchange Mass Spectrometry.Protein and peptide letters · 2019Review
- MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining.Molecular cell · 2018Article
- Pulsed Hydrogen-Deuterium Exchange Illuminates the Aggregation Kinetics of α-Synuclein, the Causative Agent for Parkinson's Disease.ACS chemical neuroscience · 2018Article
- Interactome Analysis Reveals Regulator of G Protein Signaling 14 (RGS14) is a Novel Calcium/Calmodulin (CaJournal of proteome research · 2018Article
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Authors and funding
6 authors.
Funding
Abstract
Application of typical HDX methods to examine intrinsically disordered proteins (IDP), proteins that are natively unstructured and highly dynamic at physiological pH, is limited because of the rapid exchange of unprotected amide hydrogens with solvent. The exchange rates of these fast exchanging amides are usually faster than the shortest time scale (10 s) employed in typical automated HDX-MS experiments. Considering the functional importance of IDPs and their association with many diseases, it is valuable to develop methods that allow the study of solution dynamics of these proteins as well as the ability to probe the interaction of IDPs with their wide range of binding partners. Here, we report the application of time window expansion to the millisecond range by altering the on-exchange pH of the HDX experiment to study a well-characterized IDP; the activation domain of the nuclear receptor coactivator, peroxisome proliferator-activated receptor gamma coactivator-1 alpha (PGC-1α). This method enabled mapping the regions of PGC-1α that are stabilized upon binding the ligand binding domain (LBD) of the nuclear receptor peroxisome proliferator-activated receptor gamma (PPARγ). We further demonstrate the method's applicability to other binding partners of the IDP PGC-1α and pave the way for characterizing many other biologically important ID proteins.
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