Ramagopal, Udupi A and Ramakumar, Suryanarayanarao and Mathur, Puniti and Joshi, Ratanmani and Chauhan, Virander S (2002) Dehydrophenylalanine zippers: strong helix-helix clamping through a network of weak interactions. In: Protein Engineering, 15 (4). pp. 331-335.
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A decapeptide Boc-L-Ala-(DeltaPhe)(4)-L-Ala-(DeltaPhe)(3)-Gly-OMe (Peptide I) was synthesized to study the preferred screw sense of consecutive alpha,beta-dehydrophenylalanine (DeltaPhe) residues. Crystallographic and CD studies suggest that, despite the presence of two L-Ala residues in the sequence, the decapeptide does not have a preferred screw sense. The peptide crystallizes with two conformers per asymmetric unit, one of them a slightly distorted right-handed 3(10)-helix (X) and the other a left-handed 3(10)-helix (Y) with X and Y being antiparallel to each other. An unanticipated and interesting observation is that in the solid state, the two shape-complement molecules self-assemble and interact with an extensive network of C-H...O hydrogen bonds and pi-pi interactions, directed laterally to the helix axis with amazing regularity. Here, we present an atomic resolution picture of the weak interaction mediated mutual recognition of two secondary structural elements and its possible implication in understanding the specific folding of the hydrophobic core of globular proteins and exploitation in future work on de novo design.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Oxford University Press.|
|Keywords:||aromatic interactions;dehydrophenylalanine;de novo design;310 helix|
|Department/Centre:||Division of Information Sciences > BioInformatics Centre
Division of Physical & Mathematical Sciences > Physics
|Date Deposited:||20 Jul 2011 09:25|
|Last Modified:||20 Jul 2011 09:25|
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