THE MAKING OF A FOOTPRINT IN PROTEIN FOOTPRINTING: A REVIEW IN HONOR OF MICHAEL L. GROSS
JournalMass Spectrometry Reviews
PublisherJohn Wiley and Sons Inc.
MetadataShow full item record
AbstractWithin the past decade protein footprinting in conjunction with mass spectrometry has become a powerful and versatile means to unravel the higher order structure of proteins. Footprinting-based approaches has demonstrated the capacity to inform on interaction sites and dynamic regions that participate in conformational changes. These findings when set in a biological perspective inform on protein folding/unfolding, protein-protein interactions, and protein-ligand interactions. In this review, we will look at the contribution of Dr. Michael L. Gross to protein footprinting approaches such as hydrogen deuterium exchange mass spectrometry and hydroxyl radical protein footprinting. This review details the development of novel footprinting methods as well as their applications to study higher order protein structure. © 2020 The Authors.
Keywordhigher order structure
hydrogen deuterium exchange
hydroxyl radical protein footprinting
Identifier to cite or link to this itemhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85084462569&doi=10.1002%2fmas.21632&partnerID=40&md5=10cae0bf9f8798c2e461cf9edb5422e8; http://hdl.handle.net/10713/12805