Mass spectrometry: come of age for structural and dynamical biology
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TLDR
How molecular-level information is derived from MS experiments is described, and how it can be combined with spatial and dynamical restraints obtained from other structural biology approaches to allow hybrid studies of protein architecture and movements.About:
This article is published in Current Opinion in Structural Biology.The article was published on 2011-10-01 and is currently open access. It has received 250 citations till now.read more
Citations
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Journal ArticleDOI
Membrane proteins bind lipids selectively to modulate their structure and function
Arthur Laganowsky,Eamonn Reading,Timothy M. Allison,Martin B. Ulmschneider,Matteo T. Degiacomi,Andrew Baldwin,Carol V. Robinson +6 more
TL;DR: It is demonstrated that resistance to unfolding correlates with specific lipid-binding events, enabling a distinction to be made between lipids that merely bind from those that modulate membrane protein structure and/or function.
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Recommendations for reporting ion mobility Mass Spectrometry measurements
Valérie Gabelica,Alexandre A. Shvartsburg,Carlos Afonso,Perdita E. Barran,Justin L. P. Benesch,Christian Bleiholder,Michael T. Bowers,Aivett Bilbao,Matthew F. Bush,J. Larry Campbell,Iain D. G. Campuzano,Tim J. Causon,Brian H. Clowers,Colin S. Creaser,Edwin De Pauw,Johann Far,Francisco Fernandez-Lima,John C. Fjeldsted,Kevin Giles,Michael Groessl,Christopher J. Hogan,Stephan Hann,Hugh I. Kim,Ruwan T. Kurulugama,Jody C. May,John A. McLean,Kevin Pagel,Keith Richardson,Mark E. Ridgeway,Frédéric Rosu,Frank Sobott,Konstantinos Thalassinos,Stephen J. Valentine,Thomas Wyttenbach +33 more
TL;DR: A guide to ion mobility mass spectrometry experiments, which covers both linear and nonlinear methods: what is measured, how the measurements are done, and how to report the results, including the uncertainties of mobility and collision cross section values.
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Photodissociation mass spectrometry: new tools for characterization of biological molecules.
TL;DR: This review focuses on many of the key developments in photodissociation mass spectrometry over the past decade with a particular emphasis on its applications to biological molecules.
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Lysine-specific chemical cross-linking of protein complexes and identification of cross-linking sites using LC-MS/MS and the xQuest/xProphet software pipeline
TL;DR: A protocol that has been successfully used to generate XL-MS data from a multitude of native proteins and protein complexes is presented and should take ∼4 d to complete, and it is generally applicable to purified proteins andprotein complexes.
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Charge-State Dependent Compaction and Dissociation of Protein Complexes: Insights from Ion Mobility and Molecular Dynamics
TL;DR: It is found that all four macromolecular complexes retain their native-like topologies at low energy during collisional activation, using ion mobility-mass spectrometry (IM-MS), and this has implications for further studies as well as for understanding the process of CID and for applications to gas-phase structural biology more generally.
References
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Studying noncovalent protein complexes by electrospray ionization mass spectrometry
TL;DR: Several applications of ESI-MS are discussed, including protein interactions with metal ions and nucleic acids and subunit protein structures (quaternary structure) and mass spectrometry offers advantages in speed and sensitivity.
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Ion mobility-mass spectrometry analysis of large protein complexes.
TL;DR: Within this protocol, general approaches to data interpretation, methods of predicting whether specific model structures for a given protein assembly can be separated by ion mobility, and generalized strategies for data normalization and modeling are covered.
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Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
Summer L. Bernstein,Nicholas F. Dupuis,Noel D. Lazo,Thomas Wyttenbach,Margaret M. Condron,Gal Bitan,David B. Teplow,Joan-Emma Shea,Brandon T. Ruotolo,Carol V. Robinson,Michael T. Bowers +10 more
TL;DR: This work presents a new analysis method, ion mobility coupled with mass spectrometry, for determination of in vitro oligomer distributions and the qualitative structure of each of the aggregates, which provides a candidate in the Aβ42 dodecamer for the primary toxic species in Alzheimer's disease.
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Collision Cross Sections of Proteins and Their Complexes: A Calibration Framework and Database for Gas-Phase Structural Biology
TL;DR: This database indicates that collision cross sections in both helium and nitrogen gases can be well-correlated for larger biomolecular ions, but non-cor related differences for smaller ions can be more significant.
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Native mass spectrometry: a bridge between interactomics and structural biology.
TL;DR: The current state of native mass spectrometry technology is reviewed and several important biological applications are discussed, including high-throughput interactomics studies and current experimental challenges.