Data Resource

Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS) Centroid Data measured between 3.6 degrees C and 25.4 degrees C for the Fab Fragment of NISTmAb

Jeffrey W. Hudgens, Elyssia S. Gallagher, Ioannis Karageorgos, Kyle W. Anderson, Richard Y.-C. Huang, Guodong Chen, George M. Bou-Assaf, Alfonso Espada, Michael J. Chalmers, Eduardo Harguindey, Hui-Min Zhang, Benjamin T. Walters, Jennifer Zhang, John Venable, Caitlin Steckler, Inhee Park, Ansgar Brock, Xiaojun Lu, Ratnesh Pandey, Arun Chandramohan, Ganesh Srinivasan Anand, Sasidhar N. Nirudodhi, Justin B. Sperry, Jason C. Rouse, James A. Carroll, Kasper D. Rand, Ulrike Leurs, David D. Weis, Mohammed A. Al-Naqshabandi, Tyler S. Hageman, Daniel Deredge, Patrick L. Wintrode, Malvina Papanastasiou, John D. Lambris, Sheng Li, Sarah Urata
Contact: Jeffrey Hudgens..
Identifier: doi:10.18434/8SX3-NQ49
Version: 1.0.2... Last modified: 2018-09-28


The spreadsheet file reported herein provides centroid data, descriptive of deuterium uptake, for the Fab Fragment of NISTmAb (PDB: 5K8A) reference material, as measured by the bottom-up hydrogen-deuterium exchange mass spectrometry (HDX-MS) method. The protein sample was incubated in deuterium-rich solutions under uniform pH and salt concentrations between 3.6 degrees C and 25.4 degrees C for seven intervals ranging (0 to 14,400) s plus a control sample that simulates a Fab Fragment immersed for infinite time in D2O. The deuterium content of peptic peptide fragments were measured by mass spectrometry. These data were reported by fifteen laboratories, which conducted the measurements using orbitrap and Q-TOF mass spectrometers. The cohort reported about 78,900 centroids for 430 proteolytic peptide sequences of the heavy and light chains of NISTmAb, providing nearly 100 % coverage. The instrumentation and physical and chemical conditions under which these data were acquired are documented.
Subject Keywords: hydrogen-deuterium exchange, hydrogen exchange, HDX-MS, interlaboratory comparison, mass spectrometry, peptide, precision, proteomics, reference material, repeatability, reproducibility    

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