Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.
J Am Chem Soc. 2010 Jul 7;132(26):8838-9. doi: 10.1021/ja1020519.
Following the disruption of the covalent bond between the cysteine and flavin of Phot1LOV2-linker, the unfolded conformation of the linker folds with a time constant of 13 ms, which is considerably (approximately 10(4) times) slower than the helix formation rate measured for an alpha-helical polypeptide in solution.
在 Phot1LOV2 接头的半胱氨酸和黄素之间的共价键被破坏后，接头的展开构象以 13 毫秒的时间常数折叠，这比在溶液中测量到的α-螺旋多肽的螺旋形成速率慢得多（大约慢 10(4)倍）。
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