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

Bioconjugation methodologies have proven to play a central enabling role in the recent
development of biotherapeutics and chemical biology approaches. Recent endeavours in …

For many years, amino acid‐specific covalent labeling has been a valuable tool to study
protein structure and protein interactions, especially for systems that are difficult to study by …

Revised and updated, Chemical Reagents for Protein Modification, Third Edition is an
encyclopedic work describing the many approaches to the site-specific modification of …

Significant improvements have been made to a previously reported tryptophan modification
method using rhodium carbenoids in aqueous solution, allowing the reaction to proceed at …

Edited by renowned protein scientist and bestselling author Roger L. Lundblad, with the
assistance of Fiona M. Macdonald of CRC Press, this fifth edition of the Handbook of …

The reliability and information content of diethylpyrocarbonate (DEPC) as a covalent probe
of protein surface structure has been improved when used appropriately with mass …

Mass spectrometry has evolved as a technique suitable for the characterization of peptides
and proteins beyond their linear sequence. The advantages of mass spectrometric sample …

Despite extensive investigation of the irreversible oxidations undergone by proteins in vitro
and in vivo, the products formed from the oxidation of Trp residues remain incompletely …

Described here is the development of a mass spectrometry-based covalent labeling protocol
that utilizes the reaction of dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNSB) …