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A very extensive set of RDC measurements is used to identify correlated motions of a β sheet in the native state of the immunoglobulin-binding B1 domain of streptococcal protein G.
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A partially folded intermediate of the bacterial immunity protein Im7 with a substantial degree of non-native interactions is derived using hydrogen exchange protection factors as restraints in molecular dynamics simulations. The structure was validated by the prediction of chemical shift and Φ-value measurements.
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