Disulfide bonds, their stereospecific environment and conservation in protein structures

Bhattacharyya, Rajasri ; Pal, Debnath ; Chakrabarti, Pinak (2004) Disulfide bonds, their stereospecific environment and conservation in protein structures Protein Engineering Design & Selection, 17 (11). pp. 795-808. ISSN 1741-0126

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Official URL: http://peds.oxfordjournals.org/cgi/content/abstrac...

Related URL: http://dx.doi.org/10.1093/protein/gzh093


We studied the specificity of the non-bonded interaction in the environment of 572 disulfide bonds in 247 polypeptide chains selected from the Protein Data Bank. The preferred geometry of interaction of peptide oxygen atoms is along the back of the two covalent bonds at the sulfur atom of half cystine. With aromatic residues the geometries that direct one of the sulfur lone pair of electrons into the aromatic Π-system are avoided; an orientation in which the sulfide plane is normal or inclined to the aromatic plane and on top of its edge is normally preferred. The importance of the S···aromatic interaction is manifested in the high degree of its conservation across members in homologous protein families. These interactions, while providing extra overall stability to the native fold and reducing the accessibility of the disulfide bond and thereby preventing exchange reactions, also set the orientation of the conserved aromatic rings for further interactions and binding to another molecule. The conformational features and the mode of interactions of disulfide bridges should be useful for molecular design and protein engineering experiments.

Item Type:Article
Source:Copyright of this article belongs to Oxford University Press.
Keywords:Conservation Of Interaction; Disulfide Bond; Protein Stability; S···aromatic Interaction; S···O Interaction
ID Code:21445
Deposited On:22 Nov 2010 11:24
Last Modified:17 May 2016 05:39

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