Abstract
Stabilization of the tertiary protein structure is most often attributed to hydrophobic interactions, although this type of interaction is not specifically reflected in protein force fields. Initial attempts to extend the analysis of traditional nonbinding interactions with factors representing hydrophobic interactions (Levitt 1976) were not particularly successful, even though the influence of the aqueous environment on molecular dynamics cannot be underestimated in respect to experimental observations.
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Banach, M., Konieczny, L., Roterman-Konieczna, I. (2013). Can the Structure of the Hydrophobic Core Determine the Complexation Site?. In: Roterman-Konieczna, I. (eds) Identification of Ligand Binding Site and Protein-Protein Interaction Area. Focus on Structural Biology, vol 8. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-5285-6_3
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