| Combined techniques in mass spectrometry and computational chemistry provide novel characterizations for the mechanism and thermodynamics of binding interactions and decomposition reactions within small biological systems related to enzymatic function, ageing, and disease. Chapter 1 examines Na+ complexes of the deamidation and dehydration products of the acidic amino acids, aspartic acid (Asp) and glutamic acid (Glu), as well as their amide derivatives, asparagine (Asn), glutamine (Gln). Chapters 2 and 3 examine the details of Na+ and K+ binding, respectively, to the intact amino acids Asp. Glu, Asn, and Gln. These chapters investigate structural trends among the amino acid complexes and also between Na + and K+. Chapter 4 investigates the unique secondary deamidation reaction of Na+(Asn). The experimental analysis section of this chapter introduces advanced methods for combined analysis of competing and sequential reaction processes. In Chapter 5, Na+ binding to the simple monosaccharides glucose (Glc), galactose (Gal), arabinose (Ara), and xylose (Xyl) is examined. Chapter 6 investigates the decomposition of protonated Asn through deamidation and (H2O + CO) loss processes. This chapter introduces rigorous data analysis methods for determination of branching ratios among coupled reaction products. Lastly, Chapter 7 examines gas phase structures of cationized asparagine (Asn) in complexes with H+, Li+, Na+, K+, Rb+, Cs+, and Ba2 + with infrared multiphoton dissociation (IRMPD) action spectroscopy utilizing light generated by the free electron laser for infrared experiments (FELIX). |
