Article
Solution structures and backbone dynamics of the ribosomal protein S6 and its permutant P(54-55).
Protein science : a publication of the Protein Society - 1 Jan 2010
Ohman Anders, Oman Tommy, Oliveberg Mikael
Abstract excerpt
The ribosomal protein S6 from Thermus thermophilus has served as a model system for the study of protein folding, especially for understanding the effects of circular permutations of secondary structure elements. This study presents the structure of a permutant protein, the 96-residue P(54-55), and the structure of its 101-residue parent protein S6(wt) in solution. The data also characterizes the effects of...
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