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 con...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 Cowburn, 2016).展开更多
基金This work was supported by the National Nature Science Foundationof China grant 31330019(Z.-J.L),11575021(H.L.),U1530401(H.L.),U1430237(H.L.)and 31500593(G.S.)the Ministry of Science and Technology of China grants 2014CB910400(Z.-J.L)and2015CB910104(Z.-J.L)This research work is supported by aTianhe-2JK computing time award at the Beijing Computational Research Center(CSRC).
文摘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 Cowburn, 2016).
