2007
Dispersive interactions govern strong thermal stability of a protein
VONDRÁŠEK, Jiří, Tomáš KUBAŘ, Francis E. JENNEY, JR., Michael W.W. ADAMS, Milan KOŽÍŠEK et. al.Základní údaje
Originální název
Dispersive interactions govern strong thermal stability of a protein
Název česky
Disperzní interakce determinují velkou termální stabilitu proteinu
Autoři
VONDRÁŠEK, Jiří (203 Česká republika), Tomáš KUBAŘ (203 Česká republika), Francis E. JENNEY, JR. (840 Spojené státy), Michael W.W. ADAMS (840 Spojené státy), Milan KOŽÍŠEK (203 Česká republika), Jiří ČERNÝ (203 Česká republika), Vladimír SKLENÁŘ (203 Česká republika, garant) a Pavel HOBZA (203 Česká republika)
Vydání
Chemistry- A European Journal, 2007, 0947-6539
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10610 Biophysics
Stát vydavatele
Německo
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 5.330
Kód RIV
RIV/00216224:14310/07:00022789
Organizační jednotka
Přírodovědecká fakulta
Klíčová slova anglicky
ab initio calculations; hydrophobic core; hydrophobic effect; molecular modeling; NMR spectroscopy
Štítky
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 20. 6. 2008 12:55, prof. RNDr. Vladimír Sklenář, DrSc.
V originále
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. NMR experiments have shown that the only part of the protein affected by mutation is the reasonably rearranged hydrophobic core. It is hence concluded that stabilisation energies, which are dominated by London dispersion, represent the main source of stability of this protein.
Česky
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. NMR experiments have shown that the only part of the protein affected by mutation is the reasonably rearranged hydrophobic core. It is hence concluded that stabilisation energies, which are dominated by London dispersion, represent the main source of stability of this protein.
Návaznosti
| LC06030, projekt VaV |
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| MSM0021622413, záměr |
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