Stretching and unfolding of multidomain biopolymers: a statistical mechanics theory of titin.

Abstract:

:Single-molecule manipulation has allowed the forced unfolding of multidomain proteins. Here we develop a theory that not only explains these experiments, but also points out a number of difficulties in their interpretation and makes suggestions for further experiments. Our theory is valid for essentially any molecule that can be unfolded in the AFM: as an example we present force-extension curves for the unfolding of both titin and RNA hairpins. For titin we reproduce force-extension curves, the dependence of break force on pulling speed, and break-force distributions, and also validate two common experimental views: unfolding titin Ig domains can be explained as stepwise increases in contour length, and increasing force peaks in native Ig sequences represent a hierarchy of bond strengths.

journal_name

Phys Biol

journal_title

Physical biology

authors

Staple DB,Payne SH,Reddin AL,Kreuzer HJ

doi

10.1088/1478-3975/6/2/025005

subject

Has Abstract

pub_date

2009-07-01 00:00:00

pages

025005

issue

2

eissn

1478-3967

issn

1478-3975

pii

S1478-3975(09)90606-9

journal_volume

6

pub_type

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