PROTON-TRANSFER IN ARGININE-CARBOXYLATE INTERACTIONS

• Type: Article in International Scientific Journal
• Date: 1995

Authors

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

Journal

Title: Chemical Physics Letters

Vol. 245

Pages: 498-502

ISSN: 0009-2614

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 14 Citations

Scopus - 15 Citations

Scientific classification

FOS: Natural sciences > Chemical sciences

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 5