Hydrogen bonds of nucleic acids and local motions of proteins studied by nuclear spin relaxation
In my thesis I shall focus on the development of new NMR experimental methods to study structure and internal motions of two kinds of biological polymers, viz. proteins and nucleic acids. I shall investigate the anisotropic local motions of peptide planes and locate amide protons in proteins by measuring three dipole-dipole cross-correlated relaxation rate constants of single-quantum coherences involving the peptide backbone nuclei. I shall also estimate the internucleotide hydrogen bond lengths in nucleic acids from the measurement of the longitudinal auto-relaxation rate constants of both donor and acceptor nitrogen-15 nuclei of Watson-Crick base pairs. Finally I shall measure and discuss the temperature dependence of internucleotide nitrogen-nitrogen scalar couplings in nucleic acids.
Section de chimie et génie chimique
Faculté des sciences de base
Institut des sciences et ingénierie chimiques
Jury: Bernhard Brutscher, Stephan Grzesiek, Lothar Helm, Ursula Röthlisberger
Public defense: 2004-12-17
Record created on 2005-03-16, modified on 2016-08-08