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Titolo:
Modeling the deamidation of asparagine residues via succinimide intermediates
Autore:
Konuklar, FAS; Aviyente, V; Sen, TZ; Bahar, I;
Indirizzi:
Bogazici Univ, Dept Chem, TR-80815 Bebek, Istanbul, Turkey Bogazici Univ Bebek Istanbul Turkey TR-80815 0815 Bebek, Istanbul, Turkey Bogazici Univ, Ctr Polymer Res, TR-80815 Bebek, Istanbul, Turkey Bogazici Univ Bebek Istanbul Turkey TR-80815 0815 Bebek, Istanbul, Turkey
Titolo Testata:
JOURNAL OF MOLECULAR MODELING
fascicolo: 5, volume: 7, anno: 2001,
pagine: 147 - 160
SICI:
1610-2940(2001)7:5<147:MTDOAR>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANTIBODY-CATALYZED REARRANGEMENT; AB-INITIO; HYDROGEN-BONDS; PEPTIDE-BOND; DEGRADATION; RACEMIZATION; HYDROLYSIS; MECHANISM; PROTEINS; RING;
Keywords:
deamidation; succinimide; density functional theory; hydrolysis of peptides;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Aviyente, V Bogazici Univ, Dept Chem, TR-80815 Bebek, Istanbul, Turkey Bogazici Univ Bebek Istanbul Turkey TR-80815 Istanbul, Turkey
Citazione:
F.A.S. Konuklar et al., "Modeling the deamidation of asparagine residues via succinimide intermediates", J MOL MODEL, 7(5), 2001, pp. 147-160

Abstract

Density functional theory (B3LYP/6-31G*) has been used to study the cyclization, deamidation and hydrolysis reactions of a model peptide. Single point energy calculations with the polarized continuum model drastically lower the activation energy for cyclization in a basic medium. Confirmation of the experimental results that cyclization is slower than deamidation in acidic media and the opposite is true in basic media has enabled us to propose mechanisms for both processes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 07:14:41