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Bernard Bartenlian

Researcher at University of Paris-Sud

Publications -  54
Citations -  2077

Bernard Bartenlian is an academic researcher from University of Paris-Sud. The author has contributed to research in topics: Spin wave & Vicinal. The author has an hindex of 25, co-authored 53 publications receiving 1996 citations. Previous affiliations of Bernard Bartenlian include Centre national de la recherche scientifique.

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Nanoscale Magnetic Domains in Mesoscopic Magnets

TL;DR: High-resolution magnetic force microscopy studies of magnetic submicrometer-sized cobalt dots with geometrical dimensions comparable to the width of magnetic domains reveal a variety of intricate domain patterns controlled by the details of the dot geometry.
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Lateral quantization of spin waves in micron size magnetic wires

TL;DR: In this article, Brillouin light scattering spectroscopy was used to observe quantized surface spin waves in periodic arrays of magnetic Ni81Fe19 wires by means of Brilloustime Spectroscopy.
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Brillouin light scattering from quantized spin waves in micron-size magnetic wires

TL;DR: An experimental study of spin-wave quantization in arrays of micron-size magnetic wires by means of Brillouin light-scattering spectroscopy is reported in this paper, where Dipolar-dominated Damon-Eshbach spinwave modes laterally quantized in a single wire with quantized wave vector values determined by the width of the wire are studied.
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Unambiguous evidence of oscillatory magnetic coupling between Co layers in ultrahigh vacuum grown Co/Au(111)/Co trilayers.

TL;DR: The first direct evidence of oscillatory coupling in Co/Au(111)/Co trilayers grown in ultrahigh vacuum is reported and is in good agreement with theoretical predictions.
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Two-chamber AFM: probing membrane proteins separating two aqueous compartments.

TL;DR: A two-chamber atomic force microscopy setup that allows investigation of membranes spanned over nanowells, therefore separating two aqueous chambers, is designed and the elastic and yield moduli of nonsupported membranes are probed, giving access to the lateral interaction energy between proteins.