Author: Clarkson, Michael W.; Lei, Ming; Eisenmesser, Elan Z.; Labeikovsky, Wladimir; Redfield, Alfred; Kern, Dorothee
Title: Mesodynamics in the SARS nucleocapsid measured by NMR field cycling Document date: 2009_7_30
ID: zso72hho_28
Snippet: The advantages of examining relaxation properties of proteins at multiple field strengths are well-known, and due to the limitations of resolution and configuration, unidirectional expansion of measurements to higher fields has been the natural progression. Here we have expanded our sampling of the spectral density in both directions using a field-cycling apparatus and high-field magnets to measure R 1 relaxation in a heterogeneously dynamic doma.....
Document: The advantages of examining relaxation properties of proteins at multiple field strengths are well-known, and due to the limitations of resolution and configuration, unidirectional expansion of measurements to higher fields has been the natural progression. Here we have expanded our sampling of the spectral density in both directions using a field-cycling apparatus and high-field magnets to measure R 1 relaxation in a heterogeneously dynamic domain from the SARS coronavirus at atomic resolution.
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