Reference : Partial Atomic Charges Of Amino Acids In Proteins
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/63519
Partial Atomic Charges Of Amino Acids In Proteins
English
Thomas, Annick [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Milon, A. [> > > >]
Brasseur, Robert mailto [Université de Liège > > Gembloux Agro-Bio Tech >]
2004
Proteins-Structure Function and Bioinformatics
56
1
102-9
Yes (verified by ORBi)
International
0887-3585
[en] Using a semiempirical quantum mechanical procedure (FCPAC) we have calculated the
partial atomic charges of amino acids from 494 high-resolution protein
structures. To analyze the influence of the protein's environment, we considered
each residue under two conditions: either as the center of a tripeptide with PDB
structure geometry (free) or as the center of 13-16 amino acid clusters extracted
from the PDB structure (buried). The partial atomic charges from residues in
helices and in sheets were separated. The FCPAC partial atomic charges of the
Cbeta and Calpha of most residues correlate with their helix propensity,
positively for Cbeta and negatively for Calpha (r2 = 0.76 and 0.6, respectively).
The main consequence of burying residues in proteins is the polarization of the
backbone C=O bond, which is more pronounced in helices than in sheets. The
average shift of the oxygen partial charges that results from burying is -0.120
in helix and -0.084 in sheet with the charge of the proton as unit. Linear
correlations are found between the average NMR chemical shifts and the average
FCPAC partial charges of Calpha (r2 = 0.8-0.85), N (r3 = 0.67-0.72), and Cbeta
(r2 = 0.62) atoms. Correlations for helix and beta-sheet FCPAC partial charges
show parallel regressions, suggesting that the charge variations due to burying
in proteins differentiate between the dihedral angle effects and the polarization
of backbone atoms.
Researchers ; Professionals
http://hdl.handle.net/2268/63519
10.1002/prot.20093

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