Native proteins are more stable than their denatured states by

Range 5 – 10 kcal/mol
Organism Unspecified
Reference Dill KA, Ozkan SB, Shell MS, Weikl TR. The protein folding problem. Annu Rev Biophys. 2008 37 :289-316. doi: 10.1146/annurev.biophys.37.092707.153558 p.291 left column bottom paragraphPubMed ID18573083
Primary Source [238] Yang JS, Chen WW, Skolnick J, Shakhnovich EI. 2006. All-atom ab initio folding of a diverse set of proteins. Structure 15: 53–63 DOI: 10.1016/j.str.2006.11.010PubMed ID17223532
Method Primary source abstract: "Here, [investigators] show successful all-atom ab initio folding of a representative diverse set of proteins by using a minimalist transferable-energy model that consists of two-body atom-atom interactions, hydrogen bonding, and a local sequence-energy term that models sequence-specific chain stiffness. Starting from a random coil, the native-like structure was observed during replica exchange Monte Carlo (REMC) simulation for most proteins regardless of their structural classes, the lowest energy structure was close to native-in the range of 2-6 Å root-mean-square deviation (rmsd)."
Comments P.291 left column bottom paragraph: "Because native proteins are only 5–10 kcal/mol more stable than their denatured states, it is clear that no type of intermolecular force can be neglected in folding and structure prediction (primary source)."
Entered by Uri M
ID 114426