Abstract:
:Numerous biological proteins exhibit intrinsic disorder at their termini, which are associated with multifarious functional roles. Here, we show the surprising result that an increased percentage of terminal short transiently disordered regions with enhanced flexibility (TstDREF) is associated with accelerated folding rates of globular proteins. Evolutionary conservation of predicted disorder 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 intramolecular interactions and the percentage 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 the TstDREF-mediated regulation of folding kinetics that challenge protein biochemists to assess by direct experimental testing.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Mallik S,Ray T,Kundu Sdoi
10.1002/1873-3468.12725subject
Has Abstractpub_date
2017-07-01 00:00:00pages
2180-2191issue
14eissn
0014-5793issn
1873-3468journal_volume
591pub_type
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