Počet záznamů: 1
Phenylalanyl-Glycyl-Phenylalanine Tripeptide: A Model System for Aromatic-Aromatic Side Chain Interactions in Proteins
0332924 - UOCHB-X 2010 RIV US eng J - Článek v odborném periodiku
Valdés, H. - Pluháčková, Kristýna - Hobza, Pavel
Phenylalanyl-Glycyl-Phenylalanine Tripeptide: A Model System for Aromatic-Aromatic Side Chain Interactions in Proteins.
Journal of Chemical Theory and Computation. Roč. 5, č. 9 (2009), s. 2248-2256 ISSN 1549-9618
Grant CEP: GA MŠk LC512
Výzkumný záměr: CEZ:AV0Z40550506
Klíčová slova: phenylalanyl-glycyl-phenylalanine tripeptid * ab initio calculations
Kód oboru RIV: CF - Fyzikální chemie a teoretická chemie
Impakt faktor: 4.804, rok: 2009
The performance of a wide range of quantum chemical calculations for the ab initio study of realistic model systems of aromatic-aromatic side chain interactions in proteins (in particular those π-π interactions occurring between adjacent residues along the protein sequence) is here assessed on the phenylalanyl-glycyl-phenylalanine (FGF) tripeptide. Energie and geometries obtained at different levels of theory are compared with CCSD(T)/CBS benchmark energies and RI-MP2/cc-pVTZ benchmark geometries, respectively. Consequently, a protocol of calculation alternative to the very expensive CCSD(T)/CBS is proposed. In addition to this, the preferred orientation of the Phe aromatic side chains is discussed and compared with previous results on the topic.
Trvalý link: http://hdl.handle.net/11104/0178038