Article

When is the helix conformation restored after the reverse reaction of phototropin?

Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.
Journal of the American Chemical Society (Impact Factor: 10.68). 07/2010; 132(26):8838-9. DOI: 10.1021/ja1020519
Source: PubMed

ABSTRACT 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.

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