PROTON-TRANSFER IN ARGININE-CARBOXYLATE INTERACTIONS

• Tipo: Artigo em Revista Científica Internacional
• Data: 1995

Autores

MELO, A (Autor) FCUP; RAMOS, MJ (Autor) FCUP

Revista

Título: Chemical Physics Letters

Vol. 245

Páginas: 498-502

ISSN: 0009-2614

Editora: Elsevier

Indexação

ISI Web of Knowledge - 14 Citações

Scopus - 15 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Química

Outras Informações

ID Authenticus: P-001-G0H

DOI: 10.1016/0009-2614(95)01058-h

Abstract (EN): Arginine-carboxylate interactions in proteins have aroused much interest due to the important role they play in the stability of biological systems. These interactions have usually been interpreted as being associated with a zwitterionic state as opposed to a neutral one. In this work, ab initio (6-31G** basis set) calculations were carried out in vacuo on appropriate models, methylguanidinium-acetate and methylguanidine-acetic acid, to simulate the zwitterionic and neutral forms, respectively. The results obtained reveal that the neutral form is more stable than the zwitterion, i.e, proton transfer should occur with the consequent annihilation of charge in some environments, possibly hydrophobic ones.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 5