Mass spectrometry (MS) has become one of the key technologies of structural biology. In this
review, the contributions of chemical cross-linking combined with mass spectrometry (XL …

The development of new ion-activation/dissociation methods continues to be one of the most
active areas of mass spectrometry owing to the broad applications of tandem mass …

Electrospray ionization mass spectrometry (ESI-MS) is nowadays one of the cornerstones of
biomolecular mass spectrometry and proteomics. Advances in sample preparation and …

Mass spectrometry (MS) has become a crucial technique for the analysis of protein
complexes. Native MS has traditionally examined protein subunit arrangements, while …

Structural mass spectrometry (MS) is gaining increasing importance for deriving valuable
three‐dimensional structural information on proteins and protein complexes, and it …

Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …

Mass spectrometry-based methods have become increasingly important in structural biology—
in particular for large and dynamic, even heterogeneous assemblies of biomolecules. Native …

Mass spectrometry (MS) is increasingly being used to probe the structure and dynamics of
proteins and the complexes they form with other macromolecules. There are now several …

Native mass spectrometry (MS) is aimed at preserving and determining the native structure,
composition, and stoichiometry of biomolecules and their complexes from solution after they …

Current approaches to mass spectrometry (MS) require ionization of the analytes of interest.
For high-mass species, the resulting charge state distribution can be complex and difficult to …