“…When the B-helix is destabilized, it can result in partial denaturation and then protein unfolding, which can increase the possibility of amyloid accumulation. In addition, experimental evidence indicates a significant role for the N-terminal β-sheet in protein unfolding and aggregation [ [67] , [68] ]. Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Destabilizing the β-domain may result in the formation of amyloid aggregate. The binding of VAL to this region helps stabilize it and therefore prevents the formation of amyloid aggregates [ 68 ]. Most residues in presence of 100 μM have greater RMSF values than free HEWL and HEWL bound to 10 μM VAL.…”
“…When the B-helix is destabilized, it can result in partial denaturation and then protein unfolding, which can increase the possibility of amyloid accumulation. In addition, experimental evidence indicates a significant role for the N-terminal β-sheet in protein unfolding and aggregation [ [67] , [68] ]. Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Destabilizing the β-domain may result in the formation of amyloid aggregate. The binding of VAL to this region helps stabilize it and therefore prevents the formation of amyloid aggregates [ 68 ]. Most residues in presence of 100 μM have greater RMSF values than free HEWL and HEWL bound to 10 μM VAL.…”
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