Transiently disordered tails accelerate folding of globular proteins.

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 Lett

journal_title

FEBS letters

authors

Mallik S,Ray T,Kundu S

doi

10.1002/1873-3468.12725

subject

Has Abstract

pub_date

2017-07-01 00:00:00

pages

2180-2191

issue

14

eissn

0014-5793

issn

1873-3468

journal_volume

591

pub_type

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