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Single-molecule unfolding force distributions reveal a funnel-shaped energy landscape.

ABSTRACT: The protein folding process is described as diffusion on a high-dimensional energy landscape. Experimental data showing details of the underlying energy surface are essential to understanding folding. So far in single-molecule mechanical unfolding experiments a simplified model assuming a force-independent transition state has been used to extract such information. Here we show that this so-called Bell model, although fitting well to force velocity data, fails to reproduce full unfolding force distributions. We show that by applying Kramers' diffusion model, we were able to reconstruct a detailed funnel-like curvature of the underlying energy landscape and establish full agreement with the data. We demonstrate that obtaining spatially resolved details of the unfolding energy landscape from mechanical single-molecule protein unfolding experiments requires models that go beyond the Bell model.

SUBMITTER: Schlierf M

PROVIDER: S-EPMC1367298 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature

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Single-molecule unfolding force distributions reveal a funnel-shaped energy landscape.

Schlierf Michael M Rief Matthias M

Biophysical journal 20051216 4

The protein folding process is described as diffusion on a high-dimensional energy landscape. Experimental data showing details of the underlying energy surface are essential to understanding folding. So far in single-molecule mechanical unfolding experiments a simplified model assuming a force-independent transition state has been used to extract such information. Here we show that this so-called Bell model, although fitting well to force velocity data, fails to reproduce full unfolding force d ...[more]

PMID: 16361331

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