Abstract
Most proteins function as multiprotein complexes or interact with multiprotein complexes. Identification of protein-protein interactions in the context of their physiologically relevant complexes is therefore key to fully understand the cellular machinery. Here I discuss advances in chemical crosslinking methods that allow investigators to map direct subunit contacts in transient interactions with multimeric complexes. Methods discussed fall into two categories: (i) in vitro approaches with localized, inducible crosslinking reagents and (ii) in vivo approaches with unlocalized crosslinkers.
Keywords: multiprotein complexes, photoactivatable crosslinking, label transfer
Current Protein & Peptide Science
Title: New Chemical Crosslinking Methods for the Identification of Transient Protein-Protein Interactions with Multiprotein Complexes
Volume: 5 Issue: 4
Author(s): K. Melcher
Affiliation:
Keywords: multiprotein complexes, photoactivatable crosslinking, label transfer
Abstract: Most proteins function as multiprotein complexes or interact with multiprotein complexes. Identification of protein-protein interactions in the context of their physiologically relevant complexes is therefore key to fully understand the cellular machinery. Here I discuss advances in chemical crosslinking methods that allow investigators to map direct subunit contacts in transient interactions with multimeric complexes. Methods discussed fall into two categories: (i) in vitro approaches with localized, inducible crosslinking reagents and (ii) in vivo approaches with unlocalized crosslinkers.
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Cite this article as:
Melcher K., New Chemical Crosslinking Methods for the Identification of Transient Protein-Protein Interactions with Multiprotein Complexes, Current Protein & Peptide Science 2004; 5 (4) . https://dx.doi.org/10.2174/1389203043379701
DOI https://dx.doi.org/10.2174/1389203043379701 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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