Structural Proteomics–Structural Biology Led by Advancements in Mass Spectrometry Techniques

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Bioinformatics and Systems Biology".

Deadline for manuscript submissions: 20 January 2025 | Viewed by 184

Special Issue Editors

School of Medicine, Case Western Reserve University, Cleveland, OH, USA
Interests: structural biology; protein folding; mass spectrometry; biosensors; protein footprinting
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Guest Editor
Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA
Interests: X-ray; structural characterization
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Guest Editor
The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA
Interests: single-molecule 3D structure; cryo-electron tomography; macromolecular dynamics and folding
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Special Issue Information

Dear Colleagues,

Structural proteomics, driven by advancements in mass spectrometry (MS), focuses on deriving structural information from MS-based data. These structural MS methods are pivotal for characterizing protein structures, determining protein–protein interactions, and identifying protein motions. They can also be used to study proteins that are inaccessible to techniques such as NMR or X-ray crystallography. These insights are invaluable to the biopharmaceutical industry for drug development, target identification, biomarker discovery, and understanding mechanisms of drug action.

We can broadly categorize structural MS methods into two groups: peptide-based techniques and intact protein analyses.

Peptide-Centric MS Techniques

Peptide-centric MS techniques perform orthogonal three-dimensional structural analyses to complement classical biophysical methods used in structural biology. These techniques include the following:

  • Hydroxyl radical protein footprinting MS (XFP, FPOP);
  • Hydrogen/deuterium exchange MS (HDX-MS);
  • Cross-linking MS (XL-MS);
  • Covalent labeling MS.

Intact Protein Analyses

For intact protein analyses, top-down MS is used to sequence intact proteins and complement bottom-up MS by providing detailed information, such as post-translational modifications. Native MS accurately measures the mass of intact non-covalent assemblies and provides information on homogeneity, stoichiometry, and the oligomeric state of native protein complexes. Combined with ion mobility, native MS can be used to capture a snapshot of protein conformation diversity, providing global information on shapes through collision cross-section (CCS) or collision-induced unfolding (CIU) measurements.

Special Issue Call for Papers

This Special Issue aims to highlight recent innovative approaches and significant progress in structural proteomics methods. We welcome contributions on a wide range of topics, including protein-labeling approaches (XFP, FPOP, and HDX), cross-linking MS, protein interactome mapping, and intact and top-down MS. Scholars are invited to submit both original research articles and reviews.

This Special Issue promises to be a significant resource for those in the field of structural biology and mass spectrometry, offering insights into the latest methodologies and their applications.

Dr. Rohit Jain
Dr. Corie Ralston
Dr. Gang (Gary) Ren
Guest Editors

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Keywords

  • hydroxyl radical protein footprinting MS (XFP, FPOP)
  • hydrogen/deuterium exchange MS (HDX-MS)
  • cross-linking MS (XL-MS)
  • covalent labeling MS
  • top-down MS
  • native MS

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Published Papers

This special issue is now open for submission.
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