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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Wirix, Maarten J. M. Voets, Ilja K. Oude Vrielink, Anneloes S. Vredenbregt, Edgar J. D. Luiten, O. J. Bomans, Paul H. H. Sommerdijk, Nico A. J. M. |
| Description | Author Affiliation: Oude Vrielink AS ( Laboratory of Macromolecular and Organic Chemistry, Department of Chemical Engineering and Chemistry, Eindhoven University of Technology, The Netherlands); Bomans PH ( Laboratory for Materials and Interface Chemistry and Soft Matter CryoTEM Research Unit, Department of Chemical Engineering and Chemistry, Eindhoven University of Technology, The Netherlands); Vredenbregt EJ ( Research Group Coherence and Quantum Technology, Department of Applied Physics, Eindhoven University of Technology, The Netherlands. Electronic address: E.J.D.Vredenbregt@tue.nl.); Wirix MJ ( Institute for Complex Molecular Systems, Eindhoven University of Technology, The Netherlands); Sommerdijk NA ( Laboratory for Materials and Interface Chemistry and Soft Matter CryoTEM Research Unit, Department of Chemical Engineering and Chemistry, Eindhoven University of Technology, The Netherlands); Luiten OJ ( Research Group Coherence and Quantum Technology, Department of Applied Physics, Eindhoven University of Technology, The Netherlands); Voets IK ( Laboratory of Macromolecular and Organic Chemistry, Department of Chemical Engineering and Chemistry, Eindhoven University of Technology, The Netherlands) |
| Abstract | Protein interfaces play an essential role in both natural and man-made materials as stabilizers, sensors, catalysts, and selective channels for ions and small molecules. Probing the molecular arrangement within such interfaces is of prime importance to understand the relation between structure and functionality. Here we report on the preparation and characterization of large area suspended crystalline films of class II hydrophobin HFBI. This small, amphiphilic globular protein readily self-assembles at the air-water interface into a 2D hexagonal lattice which can be transferred onto a holey carbon electron microscopy grid yielding large areas of hundreds of square micrometers intact hydrophobin film spun across micron-sized holes. Fourier transform analysis of low-dose electron microscopy images and selected area electron diffraction profiles reveal a unit cell dimension a=5.6±0.1nm, in agreement with reported atomic force microscopy studies on solid substrates and grazing incidence X-ray scattering experiments at the air-water interface. These findings constitute the first step towards the utilization of large-area suspended crystalline hydrophobin films as membranes for ultrapurification and chiral separation or as biological substrates for ultrafast electron diffraction. |
| ISSN | 00219797 |
| Journal | Journal of Colloid and Interface Science |
| Volume Number | 447 |
| e-ISSN | 10957103 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-06-01 |
| Publisher Place | United States |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Fungal Proteins Chemistry Hydrophobic And Hydrophilic Interactions Trichoderma Metabolism Crystallography, X-ray Microscopy, Atomic Force Journal Article Research Support, Non-u.s. Gov't Discipline Colloid & Interface Science |
| Content Type | Text |
| Resource Type | Article |
| Subject | Surfaces, Coatings and Films Colloid and Surface Chemistry Biomaterials Electronic, Optical and Magnetic Materials |
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