Evaluating the stability of disulfide bridges in proteins: a torsional potential energy surface for diethyl disulfide

Haworth, N.L., Gready, J.E., George, R.A. and Wouters, M.A. 2007, Evaluating the stability of disulfide bridges in proteins: a torsional potential energy surface for diethyl disulfide, Molecular simulation, vol. 33, no. 6, pp. 475-485.

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Title Evaluating the stability of disulfide bridges in proteins: a torsional potential energy surface for diethyl disulfide
Author(s) Haworth, N.L.
Gready, J.E.
George, R.A.
Wouters, M.A.
Journal name Molecular simulation
Volume number 33
Issue number 6
Start page 475
End page 485
Publisher Taylor & Francis
Place of publication Colchester, England
Publication date 2007
ISSN 0892-7022
1029-0435
Summary Disulfide bonds formed by the oxidation of cysteine residues in proteins are the major form of intra- and inter-molecular covalent linkages in the polypeptide chain. To better understand the conformational energetics of this linkage, we have used the MP2(full)/6-31G(d) method to generate a full potential energy surface (PES) for the torsion of the model compound diethyl disulfide (DEDS) around its three critical dihedral angles (χ2, χ3, χ2′). The use of ten degree increments for each of the parameters resulted in a continuous, fine-grained surface. This allowed us to accurately predict the relative stabilities of disulfide bonds in high resolution structures from the Protein Data Bank. The MP2(full) surface showed significant qualitative differences from the PES calculated using the Amber force field. In particular, a different ordering was seen for the relative energies of the local minima. Thus, Amber energies are not reliable for comparison of the relative stabilities of disulfide bonds. Surprisingly, the surface did not show a minimum associated with χ2 − 60°, χ390, χ2′ − 60°. This is due to steric interference between Hα atoms. Despite this, significant populations of disulfides were found to adopt this conformation. In most cases this conformation is associated with an unusual secondary structure motif, the cross-strand disulfide. The relative instability of cross-strand disulfides is of great interest, as they have the potential to act as functional switches in redox processes.
Language eng
Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified
Socio Economic Objective 970105 Expanding Knowledge in the Environmental Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2007, Taylor & Francis
Persistent URL http://hdl.handle.net/10536/DRO/DU:30038979

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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