Correction to Microscopic Analysis of Protein Oxidative Damage: Effect of Carbonylation on Structure, Dynamics, and Aggregability of Villin Headpiece

Page 7020, Figure 5. The reported molecular hydrophobicity potential (MHP) values of the carbonylated residues aminoadipic semialdehyde (Asa) and glutamic semialdehyde (Gsa) were calculated using a different procedure than MHP values of canonical residues. Briefly, the former were calculated for amino acid side chain analogs, while the latter were calculated for complete amino acids with subsequent subtraction of the values for the backbone atoms. While both procedures are in principle sound, a direct comparison of the two sets mandates that a common procedure be used. The fully consistent, corrected values using the latter procedure are 0.62 and 0.16, for Asa and Gsa, respectively, rather than the originally reported 1.56 and 1.27. Importantly, this does not change any of the principal conclusions of the study, but does affect several of its quantitative aspects. Primarily, estimated changes in the aggregability of positively charged proteins upon carbonylation of lysine and arginine should be ln(υmut/υwt) = 2.47 ± 0.73, (Lys to Asa) and ln(υmut/υwt) = 2.78 ± 0.73 (Arg to Gsa), rather than 3.37 ± 0.73 and 3.85 ± 0.73, respectively, and 1.49 ± 0.73 and 1.80 ± 0.73, rather than 2.39 ± 0.73 and 2.87 ± 0.73 for negatively charged proteins. Additionally, in terms of MHP weights, converting Lys to Asa or Arg to Gsa is similar to mutating them to more hydrophobic methionine and threonine, respectively, rather than leucine and valine as originally reported. Accordingly, several statements in the original article should be modified as follows: