Protein Engineering, Vol. 12, No. 12, 1025-1028,
December 1999
© 1999 Oxford University Press
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Carbonyl–carbonyl interactions stabilize the partially allowed Ramachandran conformations of asparagine and aspartic acid
1 Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, 2 Cambridge Crystallographic Data Centre, 12 Union Road, Cambridge CB2 1EZ, UK
Asparagine and aspartate are known to adopt conformations in the left-handed 
-helical region and other partially allowed regions of the Ramachandran plot more readily than any other non-glycyl amino acids. The reason for this preference has not been established. An examination of the local environments of asparagine and aspartic acid in protein structures with a resolution better than 1.5 Å revealed that their side-chain carbonyls are frequently within 4 Å of their own backbone carbonyl or the backbone carbonyl of the previous residue. Calculations using protein structures with a resolution better than 1.8 Å reveal that this close contact occurs in more than 80% of cases. This carbonyl–carbonyl interaction offers an energetic sabilization for the partially allowed conformations of asparagine and aspartic acid with respect to all other non-glycyl amino acids. The non-covalent attractive interactions between the dipoles of two carbonyls has recently been calculated to have an energy comparable to that of a hydrogen bond. The preponderance of asparagine in the left-handed -helical region, and in general of aspartic acid and asparagine in the partially allowed regions of the Ramachandran plot, may be a consequence of this carbonyl–carbonyl stacking interaction.
Keywords: asparagine/aspartic acid/carbonyl stacking/propensity/Ramachandran plot
3 To whom correspondence should be addressed. E-mail: tom{at}cryst.bioc.cam.ac.uk
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