Unknown

Dataset Information

0

Order statistics theory of unfolding of multimeric proteins.


ABSTRACT: Dynamic force spectroscopy has become indispensable for the exploration of the mechanical properties of proteins. In force-ramp experiments, performed by utilizing a time-dependent pulling force, the peak forces for unfolding transitions in a multimeric protein (D)(N) are used to map the free energy landscape for unfolding for a protein domain D. We show that theoretical modeling of unfolding transitions based on combining the observed first (f(1)), second (f(2)), …, N(th) (f(N)) unfolding forces for a protein tandem of fixed length N, and pooling the force data for tandems of different length, n(1)

SUBMITTER: Zhmurov A 

PROVIDER: S-EPMC2941031 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Order statistics theory of unfolding of multimeric proteins.

Zhmurov A A   Dima R I RI   Barsegov V V  

Biophysical journal 20100901 6


Dynamic force spectroscopy has become indispensable for the exploration of the mechanical properties of proteins. In force-ramp experiments, performed by utilizing a time-dependent pulling force, the peak forces for unfolding transitions in a multimeric protein (D)(N) are used to map the free energy landscape for unfolding for a protein domain D. We show that theoretical modeling of unfolding transitions based on combining the observed first (f(1)), second (f(2)), …, N(th) (f(N)) unfolding force  ...[more]

Similar Datasets

| S-EPMC3177077 | biostudies-literature
| S-EPMC5785014 | biostudies-literature
| S-EPMC10047654 | biostudies-literature
| S-EPMC10306404 | biostudies-literature
| S-EPMC5583479 | biostudies-literature
| S-EPMC3692064 | biostudies-literature
| S-EPMC2867010 | biostudies-literature
| S-EPMC3725103 | biostudies-literature
| S-EPMC10449402 | biostudies-literature
| S-EPMC6545047 | biostudies-literature