When is the helix conformation restored after the reverse reaction of phototropin?
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.
Kawaguchi
Yuki
Y
Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.
Nakasone
Yusuke
Y
Zikihara
Kazunori
K
Tokutomi
Satoru
S
Terazima
Masahide
M
D017360:Arabidopsis; D003624:Darkness; D056949:Phototropins / Q000737:chemistry*; D017510:Protein Folding / Q000528:radiation effects; D020673:Protein Renaturation / Q000528:radiation effects; D017433:Protein Structure, Secondary / Q000528:radiation effects; D017434:Protein Structure, Tertiary
D056949:Phototropins