Skip to Content
Merck

Unexpected decoupling of stretching and bending modes in protein gels.

Physical review letters (2013-02-19)
Thomas Gibaud, Alessio Zaccone, Emanuela Del Gado, Véronique Trappe, Peter Schurtenberger
ABSTRACT

We show that gels formed by arrested spinodal decomposition of protein solutions exhibit elastic properties in two distinct frequency domains, both elastic moduli exhibiting a remarkably strong dependence on volume fraction. Considering the large difference between the protein size and the characteristic length of the network we model the gels as porous media and show that the high and low frequency elastic moduli can be respectively attributed to stretching and bending modes. The unexpected decoupling of the two modes in the frequency domain is attributed to the length scale involved: while stretching mainly relates to the relative displacement of two particles, bending involves the deformation of a strand with a thickness of the order of a thousand particle diameters.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Lysozyme human, Lysobac, recombinant, expressed in rice, ≥100,000 units/mg protein, lyophilized powder
Sigma-Aldrich
Lysozyme from human neutrophils, ≥95% (SDS-PAGE), lyophilized powder, ≥100,000 units/mg protein (E1%/280)
Sigma-Aldrich
Lysozyme from chicken egg white, BioUltra, lyophilized powder, ≥98% (SDS-PAGE), ≥40,000 units/mg protein
Sigma-Aldrich
Lysozyme from chicken egg white, powder (crystalline), 70000-140000 U/mg
Sigma-Aldrich
Lysozyme from chicken egg white, dialyzed, lyophilized, powder, ~100000 U/mg
Sigma-Aldrich
Lysozyme from chicken egg white, 10 mg/mL
Sigma-Aldrich
Lysozyme from chicken egg white, powder or granules, ≥90 %, ≥39,000 units/mg protein
Sigma-Aldrich
Lysozyme chloride form from chicken egg white, Grade VI, ≥35,000 units/mg protein (E1%/282)
Supelco
Lysozyme from chicken egg white, VETRANAL®, analytical standard