Abstract
During the process of protein folding, the regular secondary structures are formed through backbone hydrogen bonding and the side chain interact each other as well as the surrounding medium to create the more complex tertiary structure. Covalent interactions between cysteine groups, non-covalent electrostatic interactions between polar groups and van-der waals interactions between non-polar groups are commonly observed in tertiary structures. To explore the role of various forces contributing to protein stability, models based on inter-residue interactions are an attractive choice. Hence, in the present work, inter residue contact energy statistical potentials are derived and related with the surrounding hydrophobicity model. Also, the statistical potentials derived by various leading research groups are also compared with the classical surrounding hydrophobicity model. Our analysis revealed the importance of hydrophobicity as a dominant force in the protein folding process.
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