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- W1746339097 abstract "Publisher Summary This chapter focuses on the recent advances in the understanding of the folding of soluble proteins, mostly focusing on the molecular basis of co-operativity. Wrapping refers to the environmental modulation or protection of intra-molecular electrostatic interactions through an exclusion of surrounding water that takes place as the chain folds onto itself. Thus, a special many-body picture of the folding process is shown to emerge where the folding chain not only interacts with itself but also shapes the micro-environments that stabilize or destabilize the interactions. Taken together, the hydration propensity of amide and carbonyl and the dehydration-induced strengthening of their electrostatic association represent two conflictive tendencies, suggesting that there must be a crossover point in the dehydration propensity of a backbone hydrogen bond. The dehydronic force arises as a nonpolar group approaches a dehydron with a net effect of immobilizing and ultimately removing surrounding water molecules. This displacement lowers the polarizability of the microenvironment which, in turn, deshields the paired charges." @default.
- W1746339097 created "2016-06-24" @default.
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- W1746339097 date "2008-01-01" @default.
- W1746339097 modified "2023-10-14" @default.
- W1746339097 title "Folding and Wrapping Soluble Proteins: Exploring the Molecular Basis of Cooperativity and Aggregation" @default.
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- W1746339097 doi "https://doi.org/10.1016/s0079-6603(08)00602-8" @default.
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