Protein Footprinting: Auxiliary Engine to Power the Structural Biology Revolution.
footprinting
hybrid methods
mass spectrometry
proteins
structural biology
Journal
Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R
Informations de publication
Date de publication:
17 04 2020
17 04 2020
Historique:
received:
30
09
2019
revised:
07
02
2020
accepted:
10
02
2020
pubmed:
24
2
2020
medline:
31
10
2020
entrez:
24
2
2020
Statut:
ppublish
Résumé
Structural biology is entering an exciting time where many new high-resolution structures of large complexes and membrane proteins are determined regularly. These advances have been driven by over fifteen years of technology advancements, first in macromolecular crystallography, and recently in Cryo-electron microscopy. These structures are allowing detailed questions about functional mechanisms of the structures, and the biology enabled by these structures, to be addressed for the first time. At the same time, mass spectrometry technologies for protein structure analysis, "footprinting" studies, have improved their sensitivity and resolution dramatically and can provide detailed sub-peptide and residue level information for validating structures and interactions or understanding the dynamics of structures in the context of ligand binding or assembly. In this perspective, we review the use of protein footprinting to extend our understanding of macromolecular systems, particularly for systems challenging for analysis by other techniques, such as intrinsically disordered proteins, amyloidogenic proteins, and other proteins/complexes so far recalcitrant to existing methods. We also illustrate how the availability of high-resolution structural information can be a foundation for a suite of hybrid approaches to divine structure-function relationships beyond what individual techniques can deliver.
Identifiants
pubmed: 32088185
pii: S0022-2836(20)30161-3
doi: 10.1016/j.jmb.2020.02.011
pmc: PMC7245549
mid: NIHMS1578621
pii:
doi:
Substances chimiques
Amyloidogenic Proteins
0
Intrinsically Disordered Proteins
0
Multiprotein Complexes
0
Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
2973-2984Subventions
Organisme : NIBIB NIH HHS
ID : P30 EB009998
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM114056
Pays : United States
Informations de copyright
Copyright © 2020 The Authors. Published by Elsevier Ltd.. All rights reserved.
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