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

Yuki Kawaguchi; Yusuke Nakasone; Kazunori Zikihara; Satoru Tokutomi; Masahide Terazima

doi:10.1021/ja1020519

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

J Am Chem Soc. 2010 Jul 7;132(26):8838-9. doi: 10.1021/ja1020519.

Authors

Yuki Kawaguchi¹, Yusuke Nakasone, Kazunori Zikihara, Satoru Tokutomi, Masahide Terazima

Affiliation

¹ Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.

PMID: 20536129
DOI: 10.1021/ja1020519

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.

MeSH terms

Arabidopsis
Darkness
Phototropins / chemistry*
Protein Folding / radiation effects
Protein Renaturation / radiation effects
Protein Structure, Secondary / radiation effects
Protein Structure, Tertiary

Substances

Phototropins