Cross‐links between amino acid residues in close proximity can provide distance
constraints for the validation of models of the 3D structure proteins. The mapping of cross …

Abstract Acidic residues (Asp and Glu) have a high prevalence on protein surfaces, but
cross‐linking reactions targeting these residues are limited. Existing methods either require …

Mapping of weak and hence transient interactions between low-abundance interacting
molecules is still a major challenge in systems biology and protein biochemistry. Therefore …

Chemical cross-linking followed by identification of the cross-linked residues by mass
spectrometry provides structural information on protein interaction surfaces. Nevertheless …

Chemical cross‐linking, combined with mass spectrometry, has been applied to map three‐
dimensional protein structures and protein–protein interactions. Proper choice of the cross …

Come together right now with l‐DOPA: Chemical cross‐linking is widely used to study
protein–protein interactions. However, many cross‐linking agents suffer from low reactivity …

Chemical cross-linking, followed by identification of the cross-linked residues, is a powerful
approach to probe the topologies and interacting surfaces of protein assemblies. In this …

An emerging approach for studying protein-protein interaction in complexes is the
combination of chemical cross-linking and mass spectrometric analysis of the cross-linked …

The variety of protein cross-linkers developed in recent years illustrates the current
requirement for efficient reagents optimized for mass spectrometry (MS) analysis. To date …

Chemical cross-linking in combination with LC-MS/MS (XL-MS) is an emerging technology
to obtain low-resolution structural (distance) restraints of proteins and protein complexes …