A Minimal Protein Folding Model To Measure Hydrophobic and CH-pi Effects on Interactions between Nonpolar Surfaces in Water

摘要

Predicting the pathways of protein folding and quantifying the relative thermodynamic stability of intermediate and final states along these pathways constitute two of the most important challenges in modern chemistry.Such predictions are difficult because the desired relative free-energy differences among the solvated intermediates depend importantly on the sum of numerous weak intramolecular forces that contribute to each folded state,on the partition functions representative of these states,and on the effects of water and co-solutes upon these interactions.