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Home  >  Journal list  >  Polymer Journal  >  Vol.43  No.3 (2011)  >  pp.293-300

Polymer Journal
<<Previous article Vol.43  No.3 (2011)   pp.293 - 300 Next article>>

Denaturant-induced helix–coil transition of oligopeptides: theoretical and equilibrium studies of short oligopeptides C17 and AK16

Fumiaki Kanô1,5, Masaji Shinjo2,5, Zhi-jie Qin2,6, Jinsong Li2, Yoshitaka Matsumura2, Akio Shimizu3, Akio Teramoto4 and Hiroshi Kihara2
1Department of Physics, Showa University, 4562 Kamiyoshida, Fujiyoshida, Japan
2Department of Physics, Kansai Medical University, Hirakata, Japan
3Department of Environmental Engineering, Symbiosis Faculty of Engineering, Soka University, Hachioji, Japan
4Faculty of Science and Engineering, Ritsumeikan University, Shiga, Japan

A statistical mechanical theory on the effects of denaturant on the helix–coil transition of polypeptides was developed. In the proposed theory, unfolding agents were assumed to interact with the polypeptide backbone. The theoretical results were compared with the findings of guanidine-induced helix–coil transition experiments, which were conducted on short peptides (C17 and AK16). Specifically, the helix fraction and average number of helices in C17 and AK16 were estimated. Under unfolding conditions (high denaturant concentration), the number of helices in a given sequence was close to zero. The radius of gyration was measured, and the results were related to those of the proposed theory.


Keyword:
AK16; C17; helix–coil transition; α-helix; protein denaturation; unfolding by denaturant; Zimm–Bragg theory

Received: August 17, 2010 , Revised: November 10, 2010
Accepted: November 22, 2010 , Published online: February 02, 2011
© 2011 The Society of Polymer Science, Japan

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