| 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. Online. Chemistry- A European Journal. 2007, vol. 13, No 32, p. 9022-9027. ISSN 0947-6539. [citováno 2024-04-23] |
Other formats:
BibTeX
LaTeX
RIS
@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. Online. \textit{Chemistry- A European Journal}. 2007, vol.~13, No~32, p.~9022-9027. ISSN~0947-6539. [citováno 2024-04-23]
|
