Folding Mechanism of All‐β Globular Proteins

Abstract

Elucidating the mechanism for the fast folding of proteins is a challenging task. In our earlier work, we introduced the concept of “long‐range order” and related it successfully to protein folding rates. In this article, we propose a new hypothesis for the folding of two‐state all‐β proteins. The mechanism is based on the formation of a hydrophobic core, propagation of β‐strands, and the establishment of hydrogen bonds. Our hypothesis has been strengthened by the observation of a folding nucleus in β‐strands and the hydrogen‐bonding network between residues in β‐strands. Our insights on protein folding show an excellent agreement with experimental observations.

Keywords:

• Folding mechanism
• All‐β proteins
• Folding nucleus
• Hydrogen‐bonding network