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Surprising Simplicity in the Single‐Molecule Folding Mechanics of Proteins
Author(s) -
Schlierf Michael,
Rief Matthias
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200804723
Subject(s) - force spectroscopy , energy landscape , protein folding , anisotropy , polyproteins , folding (dsp implementation) , molecular mechanics , reaction coordinate , chemistry , elasticity (physics) , molecule , chemical physics , physics , classical mechanics , computational chemistry , molecular dynamics , mechanical engineering , quantum mechanics , thermodynamics , engineering , nuclear magnetic resonance , protease , enzyme
The anisotropy of the folding‐energy landscape of proteins under force can be tested with cysteine engineering. The shorter the actively contracting polypeptide (see scheme, from blue to green), the higher the force at which the protein folds. The anisotropy of the folding mechanics can be described surprisingly simply with the help of a minimal model, mainly considering the entropic elasticity of the polypeptide.