Dispersive interactions govern strong thermal stability of a protein
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F07%3A00022789" target="_blank" >RIV/00216224:14310/07:00022789 - isvavai.cz</a>
Alternative codes found
RIV/61388963:_____/07:00091972
Result on the web
—
DOI - Digital Object Identifier
—
Alternative languages
Result language
angličtina
Original language name
Dispersive interactions govern strong thermal stability of a protein
Original language description
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 affec
Czech name
Disperzní interakce determinují velkou termální stabilitu proteinu
Czech description
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 affec
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
—
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2007
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Chemistry- A European Journal
ISSN
0947-6539
e-ISSN
—
Volume of the periodical
13
Issue of the periodical within the volume
32
Country of publishing house
DE - GERMANY
Number of pages
6
Pages from-to
9022
UT code for WoS article
—
EID of the result in the Scopus database
—