Analysis of energy stabilization inside the hydrophobic core of rubredoxin

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F09%3A00010252" target="_blank" >RIV/61989592:15310/09:00010252 - isvavai.cz</a>

Alternative codes found

RIV/61388963:_____/09:00327972

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Analysis of energy stabilization inside the hydrophobic core of rubredoxin

Original language 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 structureis 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.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CF - Physical chemistry and theoretical chemistry

OECD FORD branch

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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)

Publication year

2009

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

CHEMPHYSCHEM

ISSN

1439-4235

e-ISSN

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Volume of the periodical

10

Issue of the periodical within the volume

3

Country of publishing house

DE - GERMANY

Number of pages

6

Pages from-to

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UT code for WoS article

000264229900014

EID of the result in the Scopus database

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