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dc.contributor.authorMcKenzie-Coe, Alan
dc.contributor.authorMontes, Nicholas S
dc.contributor.authorJones, Lisa M
dc.date.accessioned2021-10-28T16:53:05Z
dc.date.available2021-10-28T16:53:05Z
dc.date.issued2021-10-11
dc.identifier.urihttp://hdl.handle.net/10713/16994
dc.description.abstractHydroxyl radical protein footprinting (HRPF) coupled to mass spectrometry has been successfully used to investigate a plethora of protein-related questions. The method, which utilizes hydroxyl radicals to oxidatively modify solvent-accessible amino acids, can inform on protein interaction sites and regions of conformational change. Hydroxyl radical-based footprinting was originally developed to study nucleic acids, but coupling the method with mass spectrometry has enabled the study of proteins. The method has undergone several advancements since its inception that have increased its utility for more varied applications such as protein folding and the study of biotherapeutics. In addition, recent innovations have led to the study of increasingly complex systems including cell lysates and intact cells. Technological advances have also increased throughput and allowed for better control of experimental conditions. In this review, we provide a brief history of the field of HRPF and detail recent innovations and applications in the field. © 2021 The Authors.en_US
dc.description.urihttps://doi.org/10.1021/acs.chemrev.1c00432en_US
dc.language.isoenen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofChemical Reviewsen_US
dc.subjecthydroxyl radical protein footprinting (HRPF)en_US
dc.subject.meshMass Spectrometryen_US
dc.titleHydroxyl Radical Protein Footprinting: A Mass Spectrometry-Based Structural Method for Studying the Higher Order Structure of Proteinsen_US
dc.typeArticleen_US
dc.identifier.doi10.1021/acs.chemrev.1c00432
dc.identifier.pmid34633178
dc.source.countryUnited States


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