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Angelo Miguel Figueiredo, Sara B.-M. Whittaker, Stuart E. Knowling, Sheena E. Radford and Geoffrey R. Moore

2013-12-4 9:37:12

The diversity of possible conformational states makes it challenging to obtain a structural description of how proteins fold. Clusters of hydrophobic residues in unfolded states of a protein help determine interatomic contacts in the early stages of folding. Here, the authors describe dynamics of an Im7 variant designed to increase the helical propensity of the shortest of the four helices of the native protein and reveal the importance of conformational properties besides helical propensity. The authors also show that hydrophobic clusters in its urea-unfolded state are related to a network of highly frustrated interactions in the native state. (from:www.onlinelibrary.wiley.com)

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