Attributes | Values |
---|
rdf:type
| |
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.
- 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)
|
Title
| - Dispersive interactions govern strong thermal stability of a protein
- Dispersive interactions govern strong thermal stability of a protein (en)
|
skos:prefLabel
| - Dispersive interactions govern strong thermal stability of a protein
- Dispersive interactions govern strong thermal stability of a protein (en)
|
skos:notation
| - RIV/00216224:14310/07:00022789!RIV10-MSM-14310___
|
http://linked.open...avai/riv/aktivita
| |
http://linked.open...avai/riv/aktivity
| - P(1M0508), P(GA203/06/1727), P(GD203/05/H001), P(IAA400550510), P(LC06030), P(LC512), Z(AV0Z40550506), Z(MSM0021622413)
|
http://linked.open...iv/cisloPeriodika
| |
http://linked.open...vai/riv/dodaniDat
| |
http://linked.open...aciTvurceVysledku
| |
http://linked.open.../riv/druhVysledku
| |
http://linked.open...iv/duvernostUdaju
| |
http://linked.open...titaPredkladatele
| |
http://linked.open...dnocenehoVysledku
| |
http://linked.open...ai/riv/idVysledku
| - RIV/00216224:14310/07:00022789
|
http://linked.open...riv/jazykVysledku
| |
http://linked.open.../riv/klicovaSlova
| - ab initio calculations; hydrophobic core; hydrophobic effect; molecular modeling; NMR spectroscopy (en)
|
http://linked.open.../riv/klicoveSlovo
| |
http://linked.open...odStatuVydavatele
| - DE - Spolková republika Německo
|
http://linked.open...ontrolniKodProRIV
| |
http://linked.open...i/riv/nazevZdroje
| - Chemistry- A European Journal
|
http://linked.open...in/vavai/riv/obor
| |
http://linked.open...ichTvurcuVysledku
| |
http://linked.open...cetTvurcuVysledku
| |
http://linked.open...vavai/riv/projekt
| |
http://linked.open...UplatneniVysledku
| |
http://linked.open...v/svazekPeriodika
| |
http://linked.open...iv/tvurceVysledku
| - Hobza, Pavel
- Kožíšek, Milan
- Sklenář, Vladimír
- Vondrášek, Jiří
- Černý, Jiří
- Kubař, Tomáš
- Adams, Michael W. W.
- Jenney jr., Francis E.
|
http://linked.open...n/vavai/riv/zamer
| |
issn
| |
number of pages
| |
http://localhost/t...ganizacniJednotka
| |
is http://linked.open...avai/riv/vysledek
of | |