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1.
Nanoscale ; 14(40): 15111-15118, 2022 Oct 21.
Artículo en Inglés | MEDLINE | ID: mdl-36205255

RESUMEN

In this work we fabricate and characterize a functionalized superconducting (SC) Nb tip of a scanning tunnelling microscope (STM). The tip is functionalized with a Tetracyanoquinodimethane molecule (TCNQ) that accepts charge from the tip and develops a magnetic moment. As a consequence, in scanning tunnelling spectroscopy (STS), sharp, bias symmetric sub-gap states identified as Yu-Shiba-Rusinov (YSR) bound states appear against the featureless density of states of a metallic graphene on Ir(111) sample. Although the coupling regime of the magnetic impurity with the SC tip depends on the initial absorption configuration of the molecule, the interaction strength between the SC tip and the charged TCNQ molecule can be reversibly controlled by tuning the tip-sample distance. The controlled transition from one coupling regime to the other allows us to verify the relation between the energy scales of the two competing many-body effects for the functionalized tip. Quenching the SC state of the Nb tip with a magnetic field switches abruptly from a tip dominated by the YSR bound states to a Kondo tip.

2.
Nat Nanotechnol ; 6(3): 185-9, 2011 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-21336269

RESUMEN

Magnetoresistance is a change in the resistance of a material system caused by an applied magnetic field. Giant magnetoresistance occurs in structures containing ferromagnetic contacts separated by a metallic non-magnetic spacer, and is now the basis of read heads for hard drives and for new forms of random access memory. Using an insulator (for example, a molecular thin film) rather than a metal as the spacer gives rise to tunnelling magnetoresistance, which typically produces a larger change in resistance for a given magnetic field strength, but also yields higher resistances, which are a disadvantage for real device operation. Here, we demonstrate giant magnetoresistance across a single, non-magnetic hydrogen phthalocyanine molecule contacted by the ferromagnetic tip of a scanning tunnelling microscope. We measure the magnetoresistance to be 60% and the conductance to be 0.26G(0), where G(0) is the quantum of conductance. Theoretical analysis identifies spin-dependent hybridization of molecular and electrode orbitals as the cause of the large magnetoresistance.


Asunto(s)
Indoles/química , Magnetismo , Nanopartículas de Magnetita/química , Nanotecnología/métodos , Cobalto/química , Cristalización/métodos , Conductividad Eléctrica , Impedancia Eléctrica , Electrodos , Electrónica/métodos , Diseño de Equipo , Estudios de Factibilidad , Compuestos Férricos/química , Isoindoles , Magnetismo/instrumentación , Ensayo de Materiales/métodos , Microscopía de Túnel de Rastreo , Procesamiento de Señales Asistido por Computador
3.
J Biochem ; 144(1): 15-9, 2008 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-18420597

RESUMEN

One feature of the alpha3-peptide, which has the amino acid sequence of (Leu-Glu-Thr-Leu-Ala-Lys-Ala)(3), that distinguishes it from many other alpha-helix-forming peptides is its ability to form fibrous assemblies that can be observed by transmission electron microscopy. In this study, the effects of Ala-->Gln substitution at the e (5th) or g (7th) position in the above heptad sequence of the alpha3-peptide on the formation of alpha-helix and fibrous assemblies were investigated by circular dichroism spectral measurement and atomic force microscopy. The 5Qalpha3-peptide obtained by Ala-->Gln substitution at the e position of the alpha3-peptide was found to form very short fibrils with long-elliptical shape, whereas the 7Qalpha3-peptide with Gln residues at the g position lost its ability to form such assemblies, in spite of alpha-helix formation in both peptides; the stabilities of both peptides decreased. These results indicate that Ala residues at the g position in the heptad sequence of the alpha3-peptide are key residues for the formation of fibrous assemblies, which may be due to hydrophobic interactions between alpha-helical bundle surfaces.


Asunto(s)
Alanina/química , Oligopéptidos/química , Péptidos/química , Alanina/genética , Sustitución de Aminoácidos , Dicroismo Circular , Microscopía de Fuerza Atómica , Oligopéptidos/genética , Péptidos/genética , Estructura Secundaria de Proteína
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