"Rubredoxin from the hyperthermophile Pyrococcus furiosus (Pf Rd) is an extremely thermostable protein, which makes it an attractive subject of protein folding and stability studies. A fundamental question arises of what the reason for such extreme stability is and how it can be elucidated from a complex set of inter-atomic interactions. We addressed this issue first theoretically through a computational analysis of the hydrophobic core of the protein and its mutants including the interactions taking place inside the core. Here we show that a single mutation of one phenylalanine's residues inside the protein's hydrophobic core results in a dramatic decrease in its thermal stability. The calculated unfolding Gibbs energy as well as the stabilisation energy differences between a few core residues follow the same trend as the melting temperature of protein variants determined experimentally by microcalorimetry measurements."@en . . "RIV/00216224:14310/07:00022789!RIV10-MSM-14310___" . "\u010Cern\u00FD, Ji\u0159\u00ED" . "DE - Spolkov\u00E1 republika N\u011Bmecko" . "RIV/00216224:14310/07:00022789" . . "Dispersive interactions govern strong thermal stability of a protein" . "Dispersive interactions govern strong thermal stability of a protein"@en . "6"^^ . "417555" . . . "ab initio calculations; hydrophobic core; hydrophobic effect; molecular modeling; NMR spectroscopy"@en . . . . . . "Kuba\u0159, Tom\u00E1\u0161" . "1"^^ . . . "[E640F2D9A93D]" . . . . . . . "Dispersive interactions govern strong thermal stability of a protein" . "Chemistry- A European Journal" . "14310" . "32" . . "8"^^ . "P(1M0508), P(GA203/06/1727), P(GD203/05/H001), P(IAA400550510), P(LC06030), P(LC512), Z(AV0Z40550506), Z(MSM0021622413)" . . "Dispersive interactions govern strong thermal stability of a protein"@en . "Hobza, Pavel" . "Jenney jr., Francis E." . "13" . "Rubredoxin from the hyperthermophile Pyrococcus furiosus (Pf Rd) is an extremely thermostable protein, which makes it an attractive subject of protein folding and stability studies. A fundamental question arises of what the reason for such extreme stability is and how it can be elucidated from a complex set of inter-atomic interactions. We addressed this issue first theoretically through a computational analysis of the hydrophobic core of the protein and its mutants including the interactions taking place inside the core. Here we show that a single mutation of one phenylalanine's residues inside the protein's hydrophobic core results in a dramatic decrease in its thermal stability. The calculated unfolding Gibbs energy as well as the stabilisation energy differences between a few core residues follow the same trend as the melting temperature of protein variants determined experimentally by microcalorimetry measurements." . . "Ko\u017E\u00ED\u0161ek, Milan" . . . . "Vondr\u00E1\u0161ek, Ji\u0159\u00ED" . "0947-6539" . . "Adams, Michael W. W." . "Sklen\u00E1\u0159, Vladim\u00EDr" . .