VONDRÁŠEK, Jiří, Tomáš KUBAŘ, Francis E. JENNEY, JR., Michael W.W. ADAMS, Milan KOŽÍŠEK, Jiří ČERNÝ, Vladimír SKLENÁŘ and Pavel HOBZA. Dispersive interactions govern strong thermal stability of a protein. Chemistry- A European Journal. 2007, vol. 13, No 32, p. 9022-9027. ISSN 0947-6539. |
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@article{726934, author = {Vondrášek, Jiří and Kubař, Tomáš and Jenney, Jr., Francis E. and Adams, Michael W.W. and Kožíšek, Milan and Černý, Jiří and Sklenář, Vladimír and Hobza, Pavel}, article_number = {32}, keywords = {ab initio calculations; hydrophobic core; hydrophobic effect; molecular modeling; NMR spectroscopy}, language = {eng}, issn = {0947-6539}, journal = {Chemistry- A European Journal}, title = {Dispersive interactions govern strong thermal stability of a protein}, url = {http://www3.interscience.wiley.com/cgi-bin/fulltext/114804131/HTMLSTART}, volume = {13}, year = {2007} }
TY - JOUR ID - 726934 AU - Vondrášek, Jiří - Kubař, Tomáš - Jenney, Jr., Francis E. - Adams, Michael W.W. - Kožíšek, Milan - Černý, Jiří - Sklenář, Vladimír - Hobza, Pavel PY - 2007 TI - Dispersive interactions govern strong thermal stability of a protein JF - Chemistry- A European Journal VL - 13 IS - 32 SP - 9022 EP - 9022 SN - 09476539 KW - ab initio calculations KW - hydrophobic core KW - hydrophobic effect KW - molecular modeling KW - NMR spectroscopy UR - http://www3.interscience.wiley.com/cgi-bin/fulltext/114804131/HTMLSTART N2 - 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. ER -
VONDRÁŠEK, Jiří, Tomáš KUBAŘ, Francis E. JENNEY, JR., Michael W.W. ADAMS, Milan KOŽÍŠEK, Jiří ČERNÝ, Vladimír SKLENÁŘ and Pavel HOBZA. Dispersive interactions govern strong thermal stability of a protein. \textit{Chemistry- A European Journal}. 2007, vol.~13, No~32, p.~9022-9027. ISSN~0947-6539.
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