Abstract

Spectral density mapping provides direct access to information on protein dynamics, by the solution of the equations for heteronuclear relaxation rates, with no assumptions as to the nature of the molecule or its dynamic behaviour. Reduced spectral density mapping allows the detailed characterisation of a protein’s motions at a lower experimental burden than the full approach. Spectral density profiles may readily be interpreted to yield information on flexibility or slow conformational exchange and to describe the anisotropic nature of the molecule.

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