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We consider a model of a biomembrane with attached proteins. The membrane is represented by a near spherical continuous surface and attached proteins are described as discrete rigid structures which attach to the membrane at a finite number of points. The resulting surface minimises a quadratic elastic energy (obtained by a perturbation of the Canham-Helfrich energy) subject to the point constraints which are imposed by the attachment of the proteins. We calculate the derivative of the energy with respect to protein configurations. The proteins are constrained to move tangentially by translation and by rotation in the axis normal to a reference point. Previous studies have typically restricted themselves to a nearly flat membrane and circular inclusions. A numerically accessible representation of this derivative is derived and employed in some numerical experiments.
We consider sharp interface asymptotics for a phase field model of two phase near spherical biomembranes involving a coupling between the local mean curvature and the local composition proposed by the first and second authors. The model is motivated
In this contribution to the proceedings of the 11th Mathematical Society of Japan (MSJ) Seasonal Institute (July 2018) we give an overview of some recent work on a mathematical model for small deformations of a spherical membrane. The idea is to cons
Interactions mediated by the cell membrane between inclusions, such as membrane proteins or antimicrobial peptides, play important roles in their biological activity. They also constitute a fascinating challenge for physicists, since they test the bo
We derive and analyse an energy to model lipid raft formation on biological membranes involving a coupling between the local mean curvature and the local composition. We apply a perturbation method recently introduced by Fritz, Hobbs and the first au
Recently 1, we presented a general theory for calculat- ing the strength and properties of colloidal interactions mediated by ligand-receptor bonds (such as those that bind DNA-coated colloids). In this communication, we derive a surprisingly simple