Accession Number:

AD1047841

Title:

Acquisition of High Field Nuclear Magnetic Resonance Spectrometers for Research in Molecular Structure, Function and Dynamics

Descriptive Note:

Technical Report,10 Aug 2009,09 Aug 2010

Corporate Author:

University of Louisville Louisville United States

Report Date:

2010-09-01

Pagination or Media Count:

33.0

Abstract:

Two High-Field NMR spectrometers supported four research projects Task 1. Mechanism of conversion of uridine to pseudouridine and to 4-thiouridine. We overexpressed the active C-terminal domain of enzyme ThiI, required for 4-thiouridine modification of tRNA. The two psuedouridine synthetases, TruB and RluA convert uridine to pseudourine in tRNA. We show the two enzymes generate the same products of F5U. Task 2. Devising new nanocomposites that can enhance wound healing. We synthesized MgO nanoparticles and characterized their interactions with ATP. Task 3. Characterization of the complex between Factor XIII and fibrinogen in blood clotting. We have set up the expression system for Fbg alphaC 242-424 in Ecoli. A system that will subsequently be used to purify the expressed protein has been established. Task 4. NMR probes for elastin spectroscopy built and tested. An expression system for heterodimeric collagen has been established. The entropy of water molecules on the surface of elastin has been measured.

Subject Categories:

  • Medicine and Medical Research
  • Anatomy and Physiology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE