Novel weak alignment techniques for nuclear magnetic resonance spectroscopy and applications to biomolecular structure determination

摘要

Nuclear magnetic resonance spectroscopy has continuously been developing everudsince its introduction as a structural method in bioscience. Recently establishedudresidual dipolar coupling techniques yield information on long-range order in weaklyudaligned samples as they define the orientation of vectors between nuclei in a commonudglobal reference frame. These data complement classical short-range information andudhave a unique potential especially for the characterization of non-globular states.udThis thesis describes the development of novel methods for the weak alignment ofudbiomacromolecules in charged gels and for the measurement of long-range residualuddipolar couplings in perdeuterated proteins. These weak alignment techniques andudother nuclear magnetic resonance methods were applied to study the structure andudfolding of various proteins such as the fibritin folding nucleus, the minicollagenudcysteine rich domain and human protein tyrosine phosphatase 1B.