Chemical Cross-Linking as a Probe for the

CHEMICAL CROSS-LINKING AS A PROBE FOR THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS 

ION MOBILITY MEASUREMENTS TO STUDY PROTEIN CONFORMATIONAL CHANGES 

From the drift-time distributions obtained in this setup, information about the number of isomers can be obtained. Some examples of IMS-mass spectrometry in conformation and folding-unfolding studies are for cytochrome c [51], apomyoglobin [51], lysozyme [52], and ubiquitin [53], 

How many charge states will be observed in the ESI spectrum of the polypeptide chain PDKDFIVNPSDLVLDNKAALRDYLRQINEYFAII-GRPRF, and at what mIz values  

How many total exchangeable hydrogens and slow-exchanging backbone amide hydrogens are present in the polypeptide H2N-SEEPPISLDLTFH-LLREVLEMARAEQLAQQAHSNRK-OH  

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