ArticleJournal of the American Society for Mass Spectrometry2015
Kinetic intermediates of holo- and apo-myoglobin studied using HDX-TIMS-MS and molecular dynamic simulations.
Article in Journal of the American Society for Mass Spectrometry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Native-Like Protein Structures in Vacuo: Steric Cooperativity as a Kinetic Barrier to Denaturation.JACS Au · 2026Article
- Histone Analysis Using Mobility- and Mass-Selected Ultraviolet Photodissociation in Tandem with Ultra-High-Resolution Mass Spectrometry.Analytical chemistry · 2025Article
- Top-Down Structural Characterization of Native Ubiquitin Combining Solution-Stable Isotope Labeling, Trapped Ion Mobility Spectrometry, and Tandem Electron Capture Dissociation Mass Spectrometry.Analytical chemistry · 2024Article
- Structural Heterogeneity of Human Histone H2A.1.The journal of physical chemistry. B · 2021Article
- Salt bridges govern the structural heterogeneity of heme protein interactions and porphyrin networks: microperoxidase-11.RSC advances · 2020Article
- Probing the Fundamentals of Native Liquid Extraction Surface Analysis Mass Spectrometry of Proteins: Can Proteins Refold during Extraction?Analytical chemistry · 2019Article
- Article
- Structural Motif Descriptors as a Way To Elucidate the Agonistic or Antagonistic Activity of Growth Hormone-Releasing Hormone Peptide Analogues.ACS omega · 2018Article
- Peptide Sequence Influence on the Conformational Dynamics and DNA binding of the Intrinsically Disordered AT-Hook 3 Peptide.Scientific reports · 2018Article
- Towards Discovery and Targeted Peptide Biomarker Detection Using nanoESI-TIMS-TOF MS.Journal of the American Society for Mass Spectrometry · 2018Article
- Discovery and targeted monitoring of polychlorinated biphenyl metabolites in blood plasma using LC-TIMS-TOF MS.International journal of mass spectrometry · 2018Article
- Conformational Landscapes of Ubiquitin, Cytochrome c, and Myoglobin: Uniform Field Ion Mobility Measurements in Helium and Nitrogen Drift Gas.International journal of mass spectrometry · 2018Article
- Fast and Effective Ion Mobility-Mass Spectrometry Separation of d-Amino-Acid-Containing Peptides.Analytical chemistry · 2017Article
- Characterization of Intramolecular Interactions of Cytochrome c Using Hydrogen-Deuterium Exchange-Trapped Ion Mobility Spectrometry-Mass Spectrometry and Molecular Dynamics.Analytical chemistry · 2017Article
- Analysis of Photoirradiated Water Accommodated Fractions of Crude Oils Using Tandem TIMS and FT-ICR MS.Environmental science & technology · 2017Article
- Ion Mobility Collision Cross Section Compendium.Analytical chemistry · 2017Review
- Retention of Native Protein Structures in the Absence of Solvent: A Coupled Ion Mobility and Spectroscopic Study.Angewandte Chemie (International ed. in English) · 2016Article
- Structures of the kinetically trapped i-motif DNA intermediates.Physical chemistry chemical physics : PCCP · 2016Article
- Towards the Analysis of High Molecular Weight Proteins and Protein complexes using TIMS-MS.International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry · 2016Article
- Isomer Separation of Polybrominated Diphenyl Ether Metabolites using nanoESI-TIMS-MS.International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry · 2016Article
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6 authors.
Funding
Abstract
In the present work, the kinetic intermediates of holo- and apo-myoglobin were studied by correlating the ion-neutral collision cross section and time resolved H/D back exchange rate simultaneously in a trapped ion mobility spectrometer coupled to a mass spectrometer (HDX-TIMS-MS). The high mobility resolution of the TIMS cell permitted the observation of multiple IMS bands and complementary molecular dynamics simulations resulted in the assignment of candidate structures for each experimental condition studied (e.g., holo [M + 8H](+8)-[M + 9H](+9) and apo [M + 9H](+9)-[M + 19H](+19)). Inspection of the kinetic intermediates suggests that the tertiary structure of apomyoglobin unfolds quickly upon the loss of the Fe protoporphyrin IX that stabilizes the interactions between the A, G, and H helices. In the absence of the porphyrin heme, the apomyoglobin unfolds to Xn kinetic intermediates that vary in the extent of unfolding as a result of the observed charge state.
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