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  • 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. (en)
Title
  • Analysis of Energy Stabilization inside the Hydrophobic Core of Rubredoxin
  • Analysis of Energy Stabilization inside the Hydrophobic Core of Rubredoxin (en)
skos:prefLabel
  • Analysis of Energy Stabilization inside the Hydrophobic Core of Rubredoxin
  • Analysis of Energy Stabilization inside the Hydrophobic Core of Rubredoxin (en)
skos:notation
  • RIV/61388963:_____/09:00327972!RIV10-MSM-61388963
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA203/05/0009), P(GA203/06/1727), P(GD203/05/H001), P(IAA400550510), P(LC512), Z(AV0Z40550506), Z(MSM6198959216)
http://linked.open...iv/cisloPeriodika
  • 3
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
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http://linked.open...dnocenehoVysledku
  • 302862
http://linked.open...ai/riv/idVysledku
  • RIV/61388963:_____/09:00327972
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  • hydrophobic core; protein stability; SAPT method (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • DE - Spolková republika Německo
http://linked.open...ontrolniKodProRIV
  • [9B44E10C1D76]
http://linked.open...i/riv/nazevZdroje
  • ChemPhysChem
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
  • 10
http://linked.open...iv/tvurceVysledku
  • Hobza, Pavel
  • Vondrášek, Jiří
  • Berka, Karel
http://linked.open...ain/vavai/riv/wos
  • 000264229900014
http://linked.open...n/vavai/riv/zamer
issn
  • 1439-4235
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