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Updated: Sep 4, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
Published on: September 16, 2010
Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics
Oxana V Galzitskaya1, Sergiy O Garbuzynskiy, Dmitry N Ivankov
1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia. ogalzit@vega.protres.ru
Abstract:
We demonstrate that chain length is the main determinant of the folding rate for proteins with the three-state folding kinetics. The logarithm of their folding rate in water (k(f)) strongly anticorrelates with their chain length L (the correlation coefficient being -0.80). At the same time, the chain length has no correlation with the folding rate for two-state folding proteins (the correlation coefficient is -0.07). Another significant difference of these two groups of proteins is a strong anticorrelation between the folding rate and Baker's "relative contact order" for the two-state folders and the complete absence of such correlation for the three-state folders.
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