About: Dispersive interactions govern strong thermal stability of a protein

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
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	P Z
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	32
http://linked.open...vai/riv/dodaniDat	2010
http://linked.open...aciTvurceVysledku	Sklenář, Vladimír
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	417555
http://linked.open...ai/riv/idVysledku	RIV/00216224:14310/07:00022789
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	ab initio calculations; hydrophobic core; hydrophobic effect; molecular modeling; NMR spectroscopy (en)
http://linked.open.../riv/klicoveSlovo	NMR spectroscopy ab initio calculations molecular modeling hydrophobic core hydrophobic effect
http://linked.open...odStatuVydavatele	DE - Spolková republika Německo
http://linked.open...ontrolniKodProRIV	[E640F2D9A93D]
http://linked.open...i/riv/nazevZdroje	Chemistry- A European Journal
http://linked.open...in/vavai/riv/obor	BO
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	8 (xsd:int)
http://linked.open...vavai/riv/projekt	New Antivirals and Antineoplastics Biomolecular centre Center for biomolecules and complex molecular systems Experimental Study and Computer Modeling of the Structure and Function of the Complex Molecular Systems and Bio(macro)molecules Experimental and computational analysis of hydrophobic clusters in thermophilic proteins Accurate calculations of stabilization energies of stacking and hydrogen bonding: nucleic acid bases and proteins
http://linked.open...UplatneniVysledku	2007
http://linked.open...v/svazekPeriodika	13
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	Regulace biologických procesů: Chemické modulátory vybraných systémů významných pro medicínu a zemědělství Proteiny v metabolismu a při interakci organismů s prostředím
issn	0947-6539
number of pages	6 (xsd:int)
http://localhost/t...ganizacniJednotka	14310
is http://linked.open...avai/riv/vysledek of	Dispersive interactions govern strong thermal stability of a protein Dispersive interactions govern strong thermal stability of a protein Dispersive interactions govern strong thermal stability of a protein

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