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Protein solubility and conformational stability are a result of a balance of interactions both within a protein and between protein and solvent. The electrostatic solvation free energy of oligoglycines, models for the peptide backbone, becomes more favorable with an increasing length, yet longer peptides collapse due to the formation of favorable intrapeptide interactions between CO dipoles, in some cases without hydrogen bonds. The strongly repulsive solvent cavity formation is balanced by vandoi:10.5488/cmp.19.23802 pmid:28943833 pmcid:PMC5607018 fatcat:54tg3momo5b4jlv2cxn5n3fs2i