Surprising simplicity in the single-molecule folding mechanics of protein.

[摘要]：The anisotropy of the folding energy landscape of proteins such as ubiquitin (Ub) under mech. force can be tested with Cys residue engineering using single-mol. force spectroscopy. The shorter the actively contracting polypeptide, the higher the force at which the protein folds. Constructs of Ub, which folds against mech. loads applied in the N-C-terminal direction, were used in the expts. The anisotropy of the folding mechanics could be described surprisingly simply with the help of a minimal model, mainly considering the entropic elasticity of the polypeptide.

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