Close pairs of carboxylates: a possibility of multicenter hydrogen bonds in proteins.
Protein Eng
; 16(3): 201-7, 2003 Mar.
Article
em En
| MEDLINE
| ID: mdl-12702800
ABSTRACT
Covalent attachment of hydrogen to the donor atom may be not an essential characteristic of stable hydrogen bonds. A positively charged particle (such as a proton), located between the two negatively charged residues, may lead to a stable interaction of the two negative residues. This paper analyzes close Asp-Glu pairs of residues in a large set of protein chains; 840 such pairs of residues were identified, of which 28% were stabilized by a metal ion, 12% by a positive residue nearby and 60% are likely to be stabilized by a proton. The absence of apparent structural constraints, secondary structure preferences, somewhat lower B-factors and a distinct correlation between pH and the minimal O-O distance in carboxylate pairs suggest that most of the abnormally close pairs could indeed be stabilized by a shared proton. Implications for protein stability and modeling are discussed.
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Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
/
Proteínas
/
Aminoácidos Acídicos
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Protein Eng
Assunto da revista:
BIOQUIMICA
/
BIOTECNOLOGIA
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
Estados Unidos