CONTRIBUTION OF UNUSUAL ARGININE-ARGININE SHORT-RANGE INTERACTIONS TO STABILIZATION AND RECOGNITION IN PROTEINS

• Type: Article in International Scientific Journal
• Date: 1994

Authors

MAGALHAES, A (Author) FCUP; MAIGRET, B (Author) Other; HOFLACK, J (Author) Other; GOMES, JANF (Author) FCUP; SCHERAGA, HA (Author) Other

Journal

Title: Journal of Protein Chemistry

Vol. 13

Pages: 195-215

ISSN: 0277-8033

Publisher: Kluwer Academic Publishers-Plenum Publishers

Indexing

ISI Web of Knowledge - 111 Citations

Scopus - 109 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-001-KEK

DOI: 10.1007/bf01891978

Abstract (EN): Although the majority of the ion pairs found in proteins consists of two charges of opposite sign, the observation of some unusual arrangements of two arginines led us to a search of such occurrences in the Brookhaven Protein Data Bank. We have found 41 Arginine-Arginine interactions with a C-zeta... C-zeta distance Less than 5 Angstrom. Computer graphics analysis of these structures shows that most of the Arg-Arg pairs are found in the vicinity of the surface of the proteins, in an easily hydrated region. In order to determine which factors could stabilize such arrangements of species of similar charge, we have carried out AM1 semi-empirical calculations on a model of two guanidinium ions surrounded by several water molecules. The results show the existence of stable clusters with six or more water molecules, with distances beween C-zeta atoms around 3 Angstrom. The bridging role of the water molecules is an important structural and energetic feature and we find bridges of two and three molecules between the guanidinium ions. These results are in good agreement with the structures found in our search of the experimental data. Enhancement of the electrostatic potential around these clusters, when compared to one of the guanidinium ions alone, is also demonstrated.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 21