【摘 要】
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Dear Editor,A disulfide bond that formed between the thiol groups of two spatially close cysteine residues is essential for protein folding,stability,and functi
【机 构】
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National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beij
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Dear Editor,A disulfide bond that formed between the thiol groups of two spatially close cysteine residues is essential for protein folding,stability,and function (Creighton et al.,1995) (Fass,2012).Driven by conformational entropy,native disulfide bonds stabilize the conformation of protein molecules (Dill,1990),while removal of native disulfides usually causes reduced stability of the target protein (Liu and Cowbum,2016).Previous studies showed that proper introduction of disulfide bonds could stabilize the flexible region of target proteins and reduce the conformational entropy by locking the protein into single desired conformation (Matsumura et al.,1989;Craig and Dombkowski,2013).Entropy is one of the essential features for protein crystallization (Shaw et al.,2007).Propedy engineered disulfide bonds have been shown to decrease proteins entropy,thus frequently used as strategy for high-resolution structure determination.
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