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Statements

Subject Item
n2:RIV%2F61388963%3A_____%2F09%3A00327972%21RIV10-MSM-61388963
rdf:type
n12:Vysledek skos:Concept
dcterms:description
The hydrophobic core of globular proteins is responsible for major stabilization of the protein tertiary structure. The prevailing amino-acid residues in the core are of aliphatic or aromatic character, and therefore, the core in a folded protein structure is mostly stabilized by noncovalent interactions of van der Waals origin between the amino-acid side chains. Herein, we present a theoretical analysis of the interaction energy between the amino acids of the hydrophobic core of the small globular protein rubredoxin (Rd) based on the symmetry-adapted perturbation theory (SAPT) method. The hydrophobic core of globular proteins is responsible for major stabilization of the protein tertiary structure. The prevailing amino-acid residues in the core are of aliphatic or aromatic character, and therefore, the core in a folded protein structure is mostly stabilized by noncovalent interactions of van der Waals origin between the amino-acid side chains. Herein, we present a theoretical analysis of the interaction energy between the amino acids of the hydrophobic core of the small globular protein rubredoxin (Rd) based on the symmetry-adapted perturbation theory (SAPT) method.
dcterms:title
Analysis of Energy Stabilization inside the Hydrophobic Core of Rubredoxin Analysis of Energy Stabilization inside the Hydrophobic Core of Rubredoxin
skos:prefLabel
Analysis of Energy Stabilization inside the Hydrophobic Core of Rubredoxin Analysis of Energy Stabilization inside the Hydrophobic Core of Rubredoxin
skos:notation
RIV/61388963:_____/09:00327972!RIV10-MSM-61388963
n3:aktivita
n14:Z n14:P
n3:aktivity
P(GA203/05/0009), P(GA203/06/1727), P(GD203/05/H001), P(IAA400550510), P(LC512), Z(AV0Z40550506), Z(MSM6198959216)
n3:cisloPeriodika
3
n3:dodaniDat
n16:2010
n3:domaciTvurceVysledku
n8:4936094 n8:2932016 n8:7358946
n3:druhVysledku
n18:J
n3:duvernostUdaju
n10:S
n3:entitaPredkladatele
n13:predkladatel
n3:idSjednocenehoVysledku
302862
n3:idVysledku
RIV/61388963:_____/09:00327972
n3:jazykVysledku
n17:eng
n3:klicovaSlova
hydrophobic core; protein stability; SAPT method
n3:klicoveSlovo
n4:protein%20stability n4:SAPT%20method n4:hydrophobic%20core
n3:kodStatuVydavatele
DE - Spolková republika Německo
n3:kontrolniKodProRIV
[9B44E10C1D76]
n3:nazevZdroje
ChemPhysChem
n3:obor
n11:CF
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
3
n3:projekt
n9:GA203%2F05%2F0009 n9:GD203%2F05%2FH001 n9:LC512 n9:GA203%2F06%2F1727 n9:IAA400550510
n3:rokUplatneniVysledku
n16:2009
n3:svazekPeriodika
10
n3:tvurceVysledku
Hobza, Pavel Berka, Karel Vondrášek, Jiří
n3:wos
000264229900014
n3:zamer
n5:AV0Z40550506 n5:MSM6198959216
s:issn
1439-4235
s:numberOfPages
6