Unusual biomolecules studied by NMR

Patricia L Jackson, Purdue University

Abstract

This work covers the NMR studies of a variety of biomolecular structures. In part one, NMR studies of small inhibitors complexed with serine proteases are discussed. $\sp{15}$N edited transferred NOEs are shown for BOC-Phe, BOC-Ala-Phe-al, and BOC-Ala-Phe-CF$\sb3$ bound to chymotrypsin. In addition, $\sp{19}$F NMR was used to show that peptidyl trifluoromethyl ketones bind to human leukocyte elastase as well as porcine pancreatic elastase. In part two a 3D NMR study of a 12 residue DNA molecule containing a GG mismatch is presented. A 3D NOESY-TOCSY spectrum and a 3D NOESY-NOESY spectrum of the dodecamer were obtained. Assignment methodologies and types of peaks observed in the 3D spectra are discussed and the complete proton assignment is made. Part three covers the NMR studies of an oligomer containing 4-dialkylamino-pyridine incorporated within a bis-(trimethyleneamine)disiloxane backbone. The oligomer has been shown to be active in the hydrolysis of p-nitrophenyl alkanoates of moderate chain lengths (C$\sb{12}$-C$\sb{16}$), with p-nitrophenyl tetradecanoate as the optimal substrate. 2D NOESY spectra were obtained under a variety of conditions. From the NMR studies a model of the substrate-oligomer complex is proposed and possible origins of the chain length specificity for substrates is discussed.

Degree

Ph.D.

Advisors

Gorenstein, Purdue University.

Subject Area

Biochemistry

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