Unknown

Dataset Information

0

Viscoelastic transition and yield strain of the folded protein.


ABSTRACT: For proteins, the mechanical properties of the folded state are directly related to function, which generally entails conformational motion. Through sub-Angstrom resolution measurements of the AC mechanical susceptibility of a globular protein we describe a new fundamental materials property of the folded state. For increasing amplitude of the forcing, there is a reversible transition from elastic to viscoelastic response. At fixed frequency, the amplitude of the deformation is piecewise linear in the force, with different slopes in the elastic and viscoelastic regimes. Effectively, the protein softens beyond a yield point defined by this transition. We propose that ligand induced conformational changes generally operate in this viscoelastic regime, and that this is a universal property of the folded state.

SUBMITTER: Wang Y 

PROVIDER: S-EPMC3234265 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature

altmetric image

Publications

Viscoelastic transition and yield strain of the folded protein.

Wang Yong Y   Zocchi Giovanni G  

PloS one 20111208 12


For proteins, the mechanical properties of the folded state are directly related to function, which generally entails conformational motion. Through sub-Angstrom resolution measurements of the AC mechanical susceptibility of a globular protein we describe a new fundamental materials property of the folded state. For increasing amplitude of the forcing, there is a reversible transition from elastic to viscoelastic response. At fixed frequency, the amplitude of the deformation is piecewise linear  ...[more]

Similar Datasets

| S-EPMC3579185 | biostudies-other
| S-EPMC8748439 | biostudies-literature
| S-EPMC26729 | biostudies-literature
| S-EPMC4569470 | biostudies-literature
| S-EPMC2890711 | biostudies-literature
| S-EPMC7486776 | biostudies-literature
| S-EPMC8228610 | biostudies-literature
2021-03-23 | GSE143832 | GEO
| S-EPMC7761198 | biostudies-literature
| S-EPMC6446595 | biostudies-literature