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Conformational contagion in a protein: Structural properties of a chameleon sequence
Author(s) -
Takano Kazufumi,
Katagiri Yoshiaki,
Mukaiyama Atsushi,
Chon Hyongi,
Matsumura Hiroyoshi,
Koga Yuichi,
Kanaya Shigenori
Publication year - 2007
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21451
Subject(s) - protein secondary structure , sequence (biology) , protein structure , chemistry , hyperthermophile , biophysics , biology , crystallography , biochemistry , archaea , gene
Certain sequences, known as chameleon sequences, take both α‐ and β‐conformations in natural proteins. We demonstrate that a wild chameleon sequence fused to the C‐terminal α‐helix or β‐sheet in foreign stable proteins from hyperthermophiles forms the same conformation as the host secondary structure. However, no secondary structural formation is observed when the sequence is attached to the outside of the secondary structure. These results indicate that this sequence inherently possesses an ability to make either α‐ or β‐conformation, depending on the sequentially neighboring secondary structure if little other nonlocal interaction occurs. Thus, chameleon sequences take on a satellite state through contagion by the power of a secondary structure. We propose this “conformational contagion” as a new nonlocal determinant factor in protein structure and misfolding related to protein conformational diseases. Proteins 2007. © 2007 Wiley‐Liss, Inc.