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Conformational change of the triple-helical structure. IV. Kinetics of the helix-folding of (Pro-Pro-Gly)n (n = 10, 12, and 15)

✍ Scribed by Kazuo Sutoh; Haruhiko Noda

Publisher
Wiley (John Wiley & Sons)
Year
1974
Tongue
English
Weight
532 KB
Volume
13
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

The kinetic curves of the helix‐refolding of (PPG)~n~ (n = 10, 12, and 15) were analyzed with an all‐or‐none model. The Arrhenius plot of the overall rate constant of the helixfolding k~F~ showed a negative activation energy at high temperature. With the aid of a sequential model, it was concluded that the reason for the anomaly was the instability of short helices (shorter than seven helical units in a trimeric molecule), and/or the more rapid rates of helix‐folding and helix‐opening for shorter helices.

The rate constant of the formation of one helical unit composed of three tripeptides at an end of a long helix was calculated to be 10^2–4^ sec^−1^. It was much smaller than that for other kinds of helices, such as an α helix (10^10^ sec^−1^) or a double helix of nucleic acids (10^7–9^sec^−1^).

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