Dataset for: Do transiently disordered and highly flexible N- and C-terminal tails accelerate the folding rates of globular proteins?

Numerous biological proteins exhibit intrinsic disorderness at their termini associated with multifarious functional roles. Here we show a surprising result that increased percent of terminal short transiently disordered regions with enhanced flexibility (TstDREF) is associated with accelerated folding rates of globular proteins. Evolutionary conservation of predicted disorderness at TstDREFs and drastic alteration of folding rates upon point-mutations suggest critical regulatory role(s) of TstDREFs in shaping the folding kinetics. TstDREFs are associated with long-range intra-molecular interactions and the percent of native secondary structural elements physically contacted by TstDREFs exhibit another surprising positive correlation with folding kinetics. These results allow us to infer probable molecular mechanisms behind TstDREF-mediated regulation of folding kinetics that challenge protein biochemists to assess by direct experimental testing.