Mechanisms of cooperativity underlying sequence-independent β-sheet formation

摘要: We investigate the formation of β-sheet structures in proteins without sequence-dependent side-chain interactions. To accomplish this, we introduce a model which explicitly incorporates both solvation effects and angular dependence (on protein backbone) hydrogen bond formation. The thermodynamics this is studied by exploring density states for entire system local couplings partially folded structure. Our results suggest that dynamics together with H-bond gives rise to generic cooperativity class systems; result explains why pathological aggregates involving cores can form from many different proteins. work provides foundation construction phenomenological models topology folding competition between native nonspecific aggregation.