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A universal matrix‐assisted laser desorption/ionization cleavable cross‐linker for protein structure analysis
Author(s) -
Müller Mathias Q.,
Zeiser Johannes J.,
Dreiocker Frank,
Pich Andreas,
Schäfer Mathias,
Sinz Andrea
Publication year - 2010
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.4812
Subject(s) - chemistry , linker , mass spectrometry , fourier transform ion cyclotron resonance , tandem mass spectrometry , ligand (biochemistry) , matrix assisted laser desorption/ionization , combinatorial chemistry , stereochemistry , desorption , biophysics , chromatography , biochemistry , receptor , organic chemistry , biology , adsorption , computer science , operating system
Abstract The concept of protein cross‐linking in combination with mass spectrometry holds great promise to derive structural information on protein conformation and protein‐protein interactions. We recently presented a dissociative amine‐reactive cross‐linker (NHS‐BuUrBu‐NHS) that is shown herein to be universally applicable to protein structure analysis under matrix‐assisted laser desorption/ionization tandem mass spectrometric (MALDI‐MS/MS) conditions, based on the examples of the peptides substance P, luteinizing hormone releasing hormone (LHRH), and the 32‐kDa ligand‐binding domain of peroxisome proliferator‐activated receptor alpha (PPARα). The characteristic fragment ion patterns and constant neutral losses of the cross‐linker greatly simplify the identification of different cross‐linked species from complex mixtures and drastically reduce the potential of identifying false‐positive cross‐links. Therefore, this cross‐linker holds an enormous potential for deriving structural information of proteins and protein complexes in a highly automated fashion. Copyright © 2010 John Wiley & Sons, Ltd.