Nematic field transfer in a two-dimensional protein fibril assembly
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Updated: Mar 27, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Sophia Jordens1, Konrad Schwenke, Ivan Usov
1Department of Health Sciences & Technology, ETH Zurich, Schmelzbergstrasse 9, 8092 Zurich, Switzerland. ed610@georgetown.edu raffaele.mezzenga@hest.ethz.ch.
Abstract:
We perform Atomic Force Microscopy and numerical simulations of a bimodal solution containing long, semiflexible β-lactoglobulin fibrils and short, flexible β-lactoglobulin linear aggregates at an air-water interface. Short aggregates orient perpendicular to fibrils at very short distances and preferentially parallel at intermediate distances. At even larger distances an isotropic distribution is observed. Parallel ordering coincides with aggregate stretching: by straightening, small aggregates are able to approach the fibrils within a distance smaller than their radius of gyration. These findings contribute to the understanding of how anisotropic interactions are transferred in two-dimensional bimodal nematic fields of biopolymers at liquid interfaces.
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