Abstract
The ability of polypeptide backbone amide hydrogens to serve as sensitive probes for conformational dynamics makes hydrogen exchange mass spectrometry (HX-MS) a powerful technique for measurement of solvent accessibility as well as energetics of hydrogen bonding in proteins. Hydrogen exchange rates are dependent on three controllable physical parameters of pH, temperature, and deuteration time which require careful calibration and precise control to observe dynamics-induced changes in hydrogen exchange. Comparative HX-MS analysis of the scaffold apolipoprotein in the free- and nanodisc-embedded states not only demonstrated the applicability of nanodisc-embedded membrane receptors for HX-MS but also provides the scaffold protein as an internal HX-MS reference standard for membrane protein HX-MS analysis. In MALDI-MS, all the fragment peptides are displayed in one spectrum without any separation. In order to carry out data analysis and interpretation, the average mass of each peptide is determined through measurement of the centroid.
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