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- W3206632447 endingPage "7561" @default.
- W3206632447 startingPage "7532" @default.
- W3206632447 abstract "Hydroxyl 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." @default.
- W3206632447 created "2021-10-25" @default.
- W3206632447 creator A5044071802 @default.
- W3206632447 creator A5070462181 @default.
- W3206632447 creator A5087560866 @default.
- W3206632447 date "2021-10-11" @default.
- W3206632447 modified "2023-09-30" @default.
- W3206632447 title "Hydroxyl Radical Protein Footprinting: A Mass Spectrometry-Based Structural Method for Studying the Higher Order Structure of Proteins" @default.
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