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 …

Proteins adopt different higher-order structures (HOS) to enable their unique biological
functions. Understanding the complexities of protein higher-order structures and dynamics …

Diazirines are widely used in photoaffinity labeling (PAL) to trap noncovalent interactions
with biomolecules. However, design and interpretation of PAL experiments is challenging …

Photoaffinity probes are routinely utilized to identify proteins that interact with small
molecules. However, despite this common usage, resolving the specific sites of these …

The advent of soft-ionization mass spectrometry for biomolecules has opened up new
possibilities for the structural analysis of proteins. Combining protein chemistry methods with …

Alkyl diazirines are frequently used in photoaffinity labeling to map small molecule–protein
interactions in target identification studies. However, the alkyl diazirines can preferentially …

The use of photo-affinity reagents for the mapping of noncovalent small molecule–protein
interactions has become widespread. Recently, several 'fully-functionalized'(FF) chemical …

While photo-cross-linking (PXL) with alkyl diazirines can provide stringent distance restraints
and offer insights into protein structures, unambiguous identification of cross-linked residues …

Using mass spectrometry (MS) to obtain information about a higher order structure of protein
requires that a protein's structural properties are encoded into the mass of that protein …

Photoaffinity labeling (PAL) is one of the few biochemical techniques that can give direct
evidence of biomolecular interactions in cells. Several photoactivatable functional groups …