Abstract
The conformational flexibility of disulfide bridges is discussed on the basis of theoretical ab initio calculations with diethyl disulfide as a model molecule. The equilibrium structure of various disulfide bridge conformations can be stretched or compressed over a surprisingly wide range of Cα⋯ Cα separations with a comparatively small energy penalty. This substantial flexibility is essential when disulfide bridges adapt to the surrounding peptide chains in the ternary structure of proteins. The total combined range for Cα⋯ Cα separations in all disulfide conformations is ca. 4.5 Å(from 3.4 to 6.9 Å), which is superior to the normal ranges for other hypothetical covalent links between polypeptide chains.
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