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Coupled folding-binding in a hydrophobic/polar protein model: impact of synergistic folding and disordered flanks.

Abstract：

:Coupled folding-binding is central to the function of many intrinsically disordered proteins, yet not fully understood. With a continuous three-letter protein model, we explore the free-energy landscape of pairs of interacting sequences and how it is impacted by 1), variations in the binding mechanism; and 2), the addition of disordered flanks to the binding region. In particular, we focus on two sequences, one with 16 and one with 35 amino acids, which make a stable dimeric three-helix bundle at low temperatures. Three distinct binding mechanisms are realized by altering the stabilities of the individual monomers: docking, coupled folding-binding of a single α-helix, and synergistic folding and binding. Compared to docking, the free-energy barrier for binding is reduced when the single α-helix is allowed to fold upon binding, but only marginally. A greater reduction is found for synergistic folding, which in addition results in a binding transition state characterized by very few interchain contacts. Disordered flanking chain segments attached to the α-helix sequence can, despite a negligible impact on the dimer stability, lead to a downhill free-energy surface in which the barrier for binding is eliminated.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Bhattacherjee A,Wallin S

doi

10.1016/j.bpj.2011.12.008

subject

Has Abstract

pub_date

2012-02-08 00:00:00

pages

569-78

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(11)05405-1

journal_volume

102

pub_type

杂志文章

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