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

Authors :: Kawaguchi, Yuki
Nakasone, Yusuke
Zikihara, Kazunori
Tokutomi, Satoru
Terazima, Masahide
Source :: Journal of the American Chemical Society. July 7, 2010, Vol. 132 Issue 26, 8838-8839
Publication Year :: 2010
Abstract: A study was conducted to understand 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 was found to be considerably slower than the helix formation rate measured for an [alpha]-helical polypeptide in solution.

Subjects :: Cysteine -- Chemical properties
Polypeptides -- Structure
Polypeptides -- Chemical properties
Protein folding -- Analysis
Chemistry

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