Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins |
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Authors: | Deepa Balasubramaniam Elizabeth A. Komives |
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Affiliation: | Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0378, USA |
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Abstract: | Amide hydrogen/deuterium exchange detected by mass spectrometry (HXMS) is seeing wider use for the identification of intrinsically disordered parts of proteins. In this review, we discuss examples of how discovery of intrinsically disordered regions and their removal can aid in structure determination, biopharmaceutical quality control, the characterization of how post-translational modifications affect weak structuring of disordered regions, the study of coupled folding and binding, and the characterization of amyloid formation. This article is part of a Special Issue entitled: Mass spectrometry in structural biology. |
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Keywords: | HXMS, hydrogen/deuterium exchange coupled to mass spectrometry IDP, intrinsically disordered protein LRP1 CT, the cytoplasmic tail of the low density lipoprotein receptor-related protein, LRP1 AR, ankyrin repeat |
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