Project: Research project

Project Details


Nuclear Magnetic Resonance (NMR) spectra of 15N and 13C nuclei in proteins
and peptides will be studied using recently developed indirect detection
techniques (HMP) which are highly sensitive. The 15N shifts will be
investigated as indicators of local hydrogen bonding, and secondary and
tertiary structure. The 13C shifts and coupling pattern will be used for
unequivocal connectivity assignment, side chain characterization, and
conformational analyses. These studies will investigate the role that
HMP-NMR can play in structural and conformational studies of proteins and
peptides related to a wide range of fundamental biochemical problems, e.g.
effector/receptor and protein nucleic acid interactions, enzyme mechanisms,
and antibody/antigen recognition. These problems are central to advancing
our knowledge of the molecular bases of disease processes. 15N-1H amide shifts will be correlated with hydrogen bonding, amide proton
exchange with solvent, and secondary structure in a range of proteins and
peptides, -- trypanothione, apamin, [1-pen] oxytocin, bovine pancreatic
trypsin inhibitor (BPTI), neurophysin, and adenylate kinase. 13C-1H shifts will be used in these compounds to extend techniques of
assignment to larger molecules than presently possible, and with 15N and 1H
shifts to investigate differences between solution and crystal structures
in BPTI, and to investigate solvent accessibility, and positions of turns. In addition to these spectroscopic analyses, modified NMR experiments will
be tested for 13C-1H correlation over several bonds using HMP-NMR. Overall, these studies should test critically how 15N and 13C spectra can
be used for conformational studies of proteins.
Effective start/end date12/31/891/1/90


  • Medicine(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology


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