Yayınlanmış 1 Ocak 2013 | Sürüm v1
Dergi makalesi Açık

Spatial ranges of driving forces are a key determinant of protein folding cooperativity and rate diversity

  • 1. Gaziantep Univ, Fac Med, Dept Biophys, TR-27310 Gaziantep, Turkey
  • 2. Ataturk Univ, Fac Sci, Dept Phys, TR-25240 Erzurum, Turkey

Açıklama

The physical basis of two-state-like folding transitions and the tremendous diversity in folding rates is elucidated by directly simulating the folding kinetics of 52 representative proteins. Relative to the results from a common modeling approach, the diversity of the simulated folding rates can be increased from similar to 10(2.1) to the experimental similar to 10(6.0) by a modest decrease in the spatial range of the attractive potential. The required theoretical range is consistent with desolvation physics and is notably much more permissive than that needed for two-state-like homopolymer collapse.

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