Exact and effective pair-wise potential for protein-ligand interactions obtained from a semiempirical energy partition

• Type: Article in International Scientific Journal
• Date: 2008

Authors

Alexandre R F Carvalho (Author) Other; Andre T Puga (Author) Other; Andre Melo (Author) FCUP

Journal

Title: International Journal Of Molecular Sciences

Vol. 9

Pages: 1652-1664

ISSN: 1661-6596

Publisher: MDPI

Indexing

ISI Web of Knowledge - 1 Citation

Scopus - 1 Citation

Scientific classification

FOS: Natural sciences > Chemical sciences

Other information

Authenticus ID: P-003-WHV

DOI: 10.3390/ijms9091652

Abstract (EN): In this work, the partition method introduced by Carvalho and Melo was used to study the complex between Cucurbita maxima trypsin inhibitor (CMTI-I) and glycerol at the AM1 level. An effective potential, combining non-bonding and polarization plus charge transfer (PLCT) terms, was introduced to evaluate the magnitude of the interaction between each amino acid and the ligand. In this case study, the nonbonding-PLCT non-compensation characterizes the stabilization energy of the association process in study. The main residues (Gly29, Cys3 and Arg5) with net attractive effects and Arg1 (with a net repulsive effect), responsible by the stability of protein-ligand complex, are associated with large nonbonding energies non-compensated by PLCT effects. The results obtained enable us to conclude that the present decomposition scheme can be used for understanding the cohesive phenomena in proteins.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 13