Hydrogen/deuterium exchange in parallel with acid/base induced protein conformational change in electrospray droplets
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Abstract
Mass spectrometry is becoming a prime tool for the study of life sciences, more specifically for protein structural biology. Indeed, protein conformation and dynamics can be studied via hydrogen/deuterium exchange (HDX) and varying pH conditions. In this perspective special feature article, Scott McLuckey and coauthors have in the source of a mass spectrometer exposed electrospray droplets containing different peptides and proteins, to vapors capable of HDX using a variety of deuterated acids and bases to induce conformational transitions and label the conformers on the time scale of the electrospray process. The results give further insights into protein conformational changes on the sub-millisecond time-scale. Scott McLuckey is Professor of Chemistry at Purdue University (West Lafayette, IN). His research interests are centered on gasphase ion chemistry and instrumentation with the goal of improving the capabilities of analytical organic and biological mass spectrometry.
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