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Transient misfolding dominates multidomain protein folding.

Nat Commun. 2015; 
BorgiaAlessandro,KemplenKatherine R,BorgiaMadeleine B,SorannoAndrea,ShammasSarah,WunderlichBengt,NettelsDaniel,BestRobert B,ClarkeJane,SchulerBenj
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摘要

Neighbouring domains of multidomain proteins with homologous tandem repeats have divergent sequences, probably as a result of evolutionary pressure to avoid misfolding and aggregation, particularly at the high cellular protein concentrations. Here we combine microfluidic-mixing single-molecule kinetics, ensemble experiments and molecular simulations to investigate how misfolding between the immunoglobulin-like domains of titin is prevented. Surprisingly, we find that during refolding of tandem repeats, independent of sequence identity, more than half of all molecules transiently form a wide range of misfolded conformations. Simulations suggest that a large fraction of these misfolds resemble an intr... More

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