Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures
 

Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures

While low temperature NMR holds great promise for the analysis of unstable samples and for sensitizing NMR detection, spectral broadening in frozen protein samples is a common experimental challenge. One hypothesis explaining the additional linewidth is that a variety of conformations are in rapid equilibrium at room temperature and become frozen, creating an inhomogeneous distribution at cryogenic temperatures. Here we investigate conformational heterogeneity by measuring the backbone torsion...

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