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 Bioljournal_title
Physical biologyauthors
Staple DB,Payne SH,Reddin AL,Kreuzer HJdoi
10.1088/1478-3975/6/2/025005subject
Has Abstractpub_date
2009-07-01 00:00:00pages
025005issue
2eissn
1478-3967issn
1478-3975pii
S1478-3975(09)90606-9journal_volume
6pub_type
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