Mass spectrometry (MS)-based proteomics methodologies have long been used for identifying and quantifying proteins from complex biological samples, with a focus on primary structures (i.e., sequence, post-translational modifications). However, higher-order structures are also critical for understanding protein functions. Despite the exciting advances in structural biology and computational methods, the high throughput structural characterization of proteins is still not trivial due to the complexity and heterogeneity that represent the “norm” of biology. Structural proteomics methods are rapid and highly versatile, thus offering complementary solutions to protein characterization especially when other techniques fail.
With the high resolving power and the speed of MS, we envision MS-based structural proteomics methodologies to have increasingly important contributions to addressing this challenge. For example, labelling-based methods (e.g., crosslinking, hydrogen/deuterium exchange, footprinting, proximity labelling) and limited proteolysis introduce conformationally-selective measurable features on proteins in their native states that can be detected and assigned to specific amino acid residues with conventional proteomics methods. Recent advances in MS hardware and hybrid instruments (e.g., ion mobility, ion activation methods, hybrid mass analyzers) also opened new possibilities to study high molecular weight intact proteins and protein complexes. Higher-order structural features such as stoichiometry, binding partners, dynamics, and even protein folds can be directly probed from the intact macromolecular complexes. In addition to experimental advances, computational methods are also indispensable for handling large datasets and effectively converting them into meaningful information. These emerging methodologies all combined provide a unique angle to the structural proteome for understanding complex biological mechanisms and aid in precision bioengineering applications.
Within this collection, we aim to highlight recent developments in:
- Experimental methodologies (sample preparation, purification, separation, etc.)
- Instrumentation (ionization, detection, activation, gas-phase chemistry, automation, etc.)
- Computational methods (software, data acquisition, data integration, bioinformatics, etc.)
- Novel applications of MS-based structural proteomics (including applying established methods on a larger scale and higher throughput, integration with non-mass spectrometry methods, etc.)
- Any related topics and combinations of the topics above
We also encourage authors to provide personal perspectives on how advances in analytical and measurement sciences have and/or will transform biological research and applications. Submissions from all sectors (academia, industry, government, etc) are welcome.
- Accepting article types: Mini Review, Original Research, Perspective, and Review.
Mass spectrometry (MS)-based proteomics methodologies have long been used for identifying and quantifying proteins from complex biological samples, with a focus on primary structures (i.e., sequence, post-translational modifications). However, higher-order structures are also critical for understanding protein functions. Despite the exciting advances in structural biology and computational methods, the high throughput structural characterization of proteins is still not trivial due to the complexity and heterogeneity that represent the “norm” of biology. Structural proteomics methods are rapid and highly versatile, thus offering complementary solutions to protein characterization especially when other techniques fail.
With the high resolving power and the speed of MS, we envision MS-based structural proteomics methodologies to have increasingly important contributions to addressing this challenge. For example, labelling-based methods (e.g., crosslinking, hydrogen/deuterium exchange, footprinting, proximity labelling) and limited proteolysis introduce conformationally-selective measurable features on proteins in their native states that can be detected and assigned to specific amino acid residues with conventional proteomics methods. Recent advances in MS hardware and hybrid instruments (e.g., ion mobility, ion activation methods, hybrid mass analyzers) also opened new possibilities to study high molecular weight intact proteins and protein complexes. Higher-order structural features such as stoichiometry, binding partners, dynamics, and even protein folds can be directly probed from the intact macromolecular complexes. In addition to experimental advances, computational methods are also indispensable for handling large datasets and effectively converting them into meaningful information. These emerging methodologies all combined provide a unique angle to the structural proteome for understanding complex biological mechanisms and aid in precision bioengineering applications.
Within this collection, we aim to highlight recent developments in:
- Experimental methodologies (sample preparation, purification, separation, etc.)
- Instrumentation (ionization, detection, activation, gas-phase chemistry, automation, etc.)
- Computational methods (software, data acquisition, data integration, bioinformatics, etc.)
- Novel applications of MS-based structural proteomics (including applying established methods on a larger scale and higher throughput, integration with non-mass spectrometry methods, etc.)
- Any related topics and combinations of the topics above
We also encourage authors to provide personal perspectives on how advances in analytical and measurement sciences have and/or will transform biological research and applications. Submissions from all sectors (academia, industry, government, etc) are welcome.
- Accepting article types: Mini Review, Original Research, Perspective, and Review.