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

Haworth, Naomi; Gready, Jill; George, RA; Wouters, M


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 (2, 3, 2'). The use of ten degree increments for each of the...[Show more]

CollectionsANU Research Publications
Date published: 2007
Type: Journal article
Source: Molecular Simulation
DOI: 10.1080/08927020701361876


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