Anisotropic deformation response of single protein molecules.

Abstract:

:Single-molecule methods have given experimental access to the mechanical properties of single protein molecules. So far, access has been limited to mostly one spatial direction of force application. Here, we report single-molecule experiments that explore the mechanical properties of a folded protein structure in precisely controlled directions by applying force to selected amino acid pairs. We investigated the deformation response of GFP in five selected directions. We found fracture forces widely varying from 100 pN up to 600 pN. We show that straining the GFP structure in one of the five directions induces partial fracture of the protein into a half-folded intermediate structure. From potential widths we estimated directional spring constants of the GFP structure and found values ranging from 1 N/m up to 17 N/m. Our results show that classical continuum mechanics and simple mechanistic models fail to describe the complex mechanics of the GFP protein structure and offer insights into the mechanical design of protein materials.

authors

Dietz H,Berkemeier F,Bertz M,Rief M

doi

10.1073/pnas.0602995103

subject

Has Abstract

pub_date

2006-08-22 00:00:00

pages

12724-8

issue

34

eissn

0027-8424

issn

1091-6490

pii

0602995103

journal_volume

103

pub_type

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