Chain length is the main determinant of the folding rate for proteins with three‐state folding kinetics | Zendy

Galzitskaya Oxana V. | Zendy; Garbuzynskiy Sergiy O. | Zendy; Ivankov Dmitry N. | Zendy; Finkelstein Alexei V. | Zendy

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Chain length is the main determinant of the folding rate for proteins with three‐state folding kinetics

Author(s) -

Galzitskaya Oxana V.,

Garbuzynskiy Sergiy O.,

Ivankov Dmitry N.,

Finkelstein Alexei V.

Publication year - 2003

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.10343

Subject(s) - folding (dsp implementation) , contact order , phi value analysis , downhill folding , protein folding , chain (unit) , kinetics , chemistry , lattice protein , logarithm , physics , mathematics , biochemistry , mathematical analysis , quantum mechanics , astronomy , electrical engineering , engineering

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. Proteins 2003;51:162–166. © 2003 Wiley‐Liss, Inc.

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