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J. Chem. Inf. Model. 2016, 56 (9), 1823−1834. DOI: 10.1021/acs.jcim.6b00399 T original manuscript described a Hamiltonian reweighting method to quickly scan a large number of force field parameters for peptide backbone dihedral angles, based on a single extensive simulation with a given force field. Parameter sets that lead to simulations with a close match to experimental data can be easily screened for. The method was applied on the GROMOS force field, parameter sets 54A7 and 54A8, searching for dihedral angle parameters that better reproduce the J-values and secondary structure propensities of all capped amino acids. To our embarrassment, we now realized that for a large portion of these mini-peptides the first peptide bond was in a cis conformation, rather than in the biologically more relevant trans conformation; see Figure 1. As the barrier for cis−trans

Correction to Optimization of Protein Backbone Dihedral Angles by Means of Hamiltonian Reweighting