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Ab‐initio and modeling study of some amino acid‐tRNA: NMR shielding and thermodynamic of solvent effect (Poster Presentation)
Author(s) -
Monajemi Hadieh,
Abdullah Wan Ahmad Tajuddin Wan,
Zain Sharifuddin
Publication year - 2007
Publication title -
pamm
Language(s) - English
Resource type - Journals
ISSN - 1617-7061
DOI - 10.1002/pamm.200701101
Subject(s) - amino acid , transfer rna , ab initio , chemistry , methionine , peptide , molecule , ribosome , peptide bond , molecular mechanics , solvent , computational chemistry , electromagnetic shielding , crystallography , organic chemistry , biochemistry , physics , rna , quantum mechanics , gene
The tRNA molecule takes suitable amino acid to the ribosome for the formation of peptide bonds. In starting the peptide chain, the first amino acid which is taken to the ribosome is methionine. We have simulated methionine‐amino acid bonding and amino acid‐tRNA bonding, using a mixed study of quantum mechanics ab‐initio and molecular mechanics. NMR shielding tensors and thermodynamic parameters and total energies are also calculated. It is important to understand the physical properties and the environmental conditions in which the dipeptides cause the tRNA to attach to a wrong amino acid. One of the properties studied is the dielectric environment of in which the bonding occurs. (© 2008 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)