BIOPHYSICS AND COMPUTATIONAL BIOLOGY, CHEMISTRY Correction for “Sequence, structure, and cooperativity in folding of elementary protein structural motifs,” by Jason K. Lai, Ginka S. Kubelka, and Jan Kubelka, which appeared in issue 32, August 11, 2015, of Proc Natl Acad Sci USA (112:9890–9895; first published July 27, 2015; 10.1073/pnas.1506309112).
The authors note that Fig. 5 appeared incorrectly. The corrected figure and its legend appear below.
Fig. 5.
Free energy profiles for experimental reaction coordinates. (A) Free energy profiles as a function of the total number of helical residues at approximately every 14 K from 274 K (blue) to 344 K (yellow) for the P22 subdomain (Left) and αtα (Right). (B) The free energy as function of the folded probability for each individual 13C-labeled stretch at two temperatures. The colors correspond to the label color scheme in Fig. 2. The apparent noise in some of the plots is due to the limited number of configurations for certain values of P, as stretches as short as two peptide bonds are considered.