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High Thermal Stability Imparted by a Designed Tandem Arg–Trp Stretch in an α‐Helical Coiled Coil
Author(s) -
Sakurai Yuuki,
Mizuno Toshihisa,
Hiroaki Hidekazu,
Gohda Keigo,
Oku Junichi,
Tanaka Toshiki
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200500806
Subject(s) - coiled coil , tandem , twist , chemistry , helix (gastropod) , crystallography , thermal stability , peptide , electromagnetic coil , chemical physics , materials science , physics , geometry , biochemistry , organic chemistry , quantum mechanics , composite material , biology , ecology , mathematics , snail
Let's twist again : A cation–π interaction between Trp and Arg is designed at the interface between two α helices of a coiled‐coil structure and stabilizes the structure more than Glu and Lys ion‐pair interactions. Two or three Trp–Arg sets form an extended array of interactions (see picture) and increase the melting temperature of the peptide.