ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structure and dynamics of protein waters revealed by radiolysis and mass spectrometry.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- The Importance of Structural Water in HDAC8 for Correct Binding Pose Applied for Drug Design of Anticancer Molecules.Anti-cancer agents in medicinal chemistry · 2024Article
- Precursor Reagent Hydrophobicity Affects Membrane Protein Footprinting.Journal of the American Society for Mass Spectrometry · 2023Article
- The Solvation of theInternational journal of molecular sciences · 2022Article
- An automated liquid jet for fluorescence dosimetry and microsecond radiolytic labeling of proteins.Communications biology · 2022Article
- Diethylpyrocarbonate Footprints a Membrane Protein in Micelles.Journal of the American Society for Mass Spectrometry · 2021Article
- Water Dynamics in Whey-Protein-Based Composite Hydrogels by Means of NMR Relaxometry.International journal of molecular sciences · 2021Article
- New high-throughput endstation to accelerate the experimental optimization pipeline for synchrotron X-ray footprinting.Journal of synchrotron radiation · 2021Article
- Inline Liquid Chromatography-Fast Photochemical Oxidation of Proteins for Targeted Structural Analysis of Conformationally Heterogeneous Mixtures.Analytical chemistry · 2021Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- Fast Protein Footprinting by X-ray Mediated Radical Trifluoromethylation.Journal of the American Society for Mass Spectrometry · 2020Article
- Development of Container Free Sample Exposure for Synchrotron X-ray Footprinting.Analytical chemistry · 2020Article
- Water molecules mediate zinc mobility in the bacterial zinc diffusion channel ZIPB.The Journal of biological chemistry · 2019Article
- The Hydration Shell of Monomeric and Dimeric Insulin Studied by Terahertz Time-Domain Spectroscopy.Biophysical journal · 2019Article
- The XFP (17-BM) beamline for X-ray footprinting at NSLS-II.Journal of synchrotron radiation · 2019Article
- Using X-ray Footprinting and Mass Spectrometry to Study the Structure and Function of Membrane Proteins.Protein and peptide letters · 2019Review
- Enhancing Structure Prediction and Design of Soluble and Membrane Proteins with Explicit Solvent-Protein Interactions.Structure (London, England : 1993) · 2017Article
- Article
- Synchrotron X-ray footprinting as a method to visualize water in proteins.Journal of synchrotron radiation · 2016Article
- Local and global structural drivers for the photoactivation of the orange carotenoid protein.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Quantitative protein topography analysis and high-resolution structure prediction using hydroxyl radical labeling and tandem-ion mass spectrometry (MS).Molecular & cellular proteomics : MCP · 2015Article
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3 authors.
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Abstract
Water is critical for the structure, stability, and functions of macromolecules. Diffraction and NMR studies have revealed structure and dynamics of bound waters at atomic resolution. However, localizing the sites and measuring the dynamics of bound waters, particularly on timescales relevant to catalysis and macromolecular assembly, is quite challenging. Here we demonstrate two techniques: first, temperature-dependent radiolytic hydroxyl radical labeling with a mass spectrometry (MS)-based readout to identify sites of bulk and bound water interactions with surface and internal residue side chains, and second, H(2)(18)O radiolytic exchange coupled MS to measure the millisecond dynamics of bound water interactions with various internal residue side chains. Through an application of the methods to cytochrome c and ubiquitin, we identify sites of water binding and measure the millisecond dynamics of bound waters in protein crevices. As these MS-based techniques are very sensitive and not protein size limited, they promise to provide unique insights into protein-water interactions and water dynamics for both small and large proteins and their complexes.
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