title: Unexpected decoupling of stretching and bending modes in protein gels.
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.
authors: Laboratoire de Physique, ENS Lyon, Université de Lyon I, CNRS/UMR 5672, 46 Allée d'Italie, 69007 Lyon, France. thomas.gibaud@ens-lyon.fr
authors: Thomas
authors: T
authors: Gibaud
authors: Alessio
authors: A
authors: Zaccone
authors: Emanuela
authors: E
authors: Del Gado
authors: Véronique
authors: V
authors: Trappe
authors: Peter
authors: P
authors: Schurtenberger
mesh_terms: D000818:Animals; D002645:Chickens; D004527:Egg Proteins / Q000737:chemistry; D004548:Elasticity; D005782:Gels / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012996:Solutions / Q000737:chemistry; D055672:Static Electricity
chemical_list: D004527:Egg Proteins; D005782:Gels; D011506:Proteins; D012996:Solutions; D009113:Muramidase