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Nuclear magnetic resonance, heteronuclear relaxation

Abstract Nuclear Magnetic Resonance (NMR) relaxation is a powerful technique that provides information about internal dynamics associated with configurational energetics in proteins, as well as site-specific information involved in conformational equilibria. In particular, N relaxation is a useful probe to characterize overall and internal backbone dynamics of proteins because the relaxation mainly reflects reorientational motion of the N-H bond vector. Over the past 20 years, experiments and protocols for analysis of N Ri, R2, and the heteronuclear N- NOE data have been well established. The development of these methods... [Pg.99]

See other pages where Nuclear magnetic resonance, heteronuclear relaxation is mentioned: [Pg.514]    [Pg.6227]    [Pg.6226]    [Pg.69]    [Pg.1652]    [Pg.18]    [Pg.925]    [Pg.210]    [Pg.127]    [Pg.144]    [Pg.89]    [Pg.329]    [Pg.487]    [Pg.1111]    [Pg.1063]   


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