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Application of Fourier transform mass spectrometry to H/D exchange of biomolecules and analysis of porphyrins by matrix-assisted laser desorption

Posted on:1998-05-04Degree:Ph.DType:Dissertation
University:University of California, DavisCandidate:Green, Melvin KirkFull Text:PDF
GTID:1464390014976523Subject:Chemistry
Abstract/Summary:
The kinetics of the gas-phase H/D exchange reactions between deuterated alcohols (D;The role of lysine and histidine residues in the H/D exchange of peptides and proteins was examined. Reactivities of a series of singly and doubly protonated bradykinin analogues can be rationalized by assuming that protonated arginine residues are unreactive, while protonated lyisne and histidine residues exchange readily. This difference is also apparent in proteins: cytochrome c, in which the predominant protonation sites are lys residues, shows a much higher exchange rate than lysozyme, in which the predominant protonation sites are arg residues.;Finally, MALDI/FTMS was investigated as an analytical tool for regular and highly strained, nonplanar porphyrins. Porphyrins could either be dissolved in toluene/ethanol and mixed with DHB in toluene/ethanol, or dissolved in CH;The role of hydrogen bonding was further examined by investigating the effect of pre-existing intracomplex hydrogen bonding on WD exchange rates between amino acids and dipeptides and CH...
Keywords/Search Tags:H/D exchange, Residues, Porphyrins
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