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. 2002 Jul 29;99(16):10359–10363. doi: 10.1073/pnas.162219099

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Copyright © 2002, The National Academy of Sciences

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Fig 3. — Parameters for predicting refolding kinetics. (A) RCO correlates to protein-refolding rates for naturally occurring proteins (open circles) but not for circular permutants of S6 (closed circle for S6, closed square for S6cp14, closed triangle for S6cp36, and closed diamond for S6cp55). Folding rates for S6 and permutants were also corrected to the average stability of the data set, where α is the solvent exposure of the transition state (bold symbols). (B) Long-range order correlates with protein-refolding rates including circular permutants of S6. (C) The percentage of short-range contacts correlates with protein-refolding rates including circular permutants of S6. Fits and correlation coefficients were calculated excluding S6 and permutants by using SIGMAPLOT 2000 (SPSS, Chicago).

Inline graphic — Parameters for predicting refolding kinetics. (A) RCO correlates to protein-refolding rates for naturally occurring proteins (open circles) but not for circular permutants of S6 (closed circle for S6, closed square for S6cp14, closed triangle for S6cp36, and closed diamond for S6cp55). Folding rates for S6 and permutants were also corrected to the average stability of the data set, where α is the solvent exposure of the transition state (bold symbols). (B) Long-range order correlates with protein-refolding rates including circular permutants of S6. (C) The percentage of short-range contacts correlates with protein-refolding rates including circular permutants of S6. Fits and correlation coefficients were calculated excluding S6 and permutants by using SIGMAPLOT 2000 (SPSS, Chicago).