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. Author manuscript; available in PMC: 2020 Feb 1.
Published in final edited form as: ACS Chem Biol. 2019 Jun 19;14(8):1677–1686. doi: 10.1021/acschembio.9b00339

Figure 3.

Figure 3.

Bar graph of the estimated enthalpic contribution of secondary interactions to the conformational stability of globular proteins. Black bars, interactions of the main chain (Figure 1); gray bars, interactions involving side chains (Figure 2). Data are from Table 1. The sum of the energies is ~27 kcal/mol per 100 residues.