We study the electronic transport across an electrostatically gated lateral junction in a HgTe quantum well, a canonical 2D topological insulator, with and without an applied magnetic field. We control the carrier density inside and outside a junction region independently and hence tune the number and nature of 1D edge modes propagating in each of those regions. Outside the bulk gap, the magnetic field drives the system to the quantum Hall regime, and chiral states propagate at the edge. In this regime, we observe fractional plateaus that reflect the equilibration between 1D chiral modes across the junction. As the carrier density approaches zero in the central region and at moderate fields, we observe oscillations in the resistance that we attribute to Fabry-Perot interference in the helical states, enabled by the broken time reversal symmetry. At higher fields, those oscillations disappear, in agreement with the expected absence of helical states when band inversion is lifted.
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http://dx.doi.org/10.1103/PhysRevLett.119.226401 | DOI Listing |
Anal Chem
January 2025
School of Molecular and Cellular Biology and Astbury Centre, University of Leeds, Leeds LS2 9JT, U.K.
Hydrogen/deuterium exchange mass spectrometry (HDX-MS) is a powerful technique to interrogate protein structure and dynamics. With the ability to study almost any protein without a size limit, including intrinsically disordered ones, HDX-MS has shown fast growing importance as a complement to structural elucidation techniques. Current experiments compare two or more related conditions (sequences, interaction partners, excipients, conformational states, etc.
View Article and Find Full Text PDFNat Commun
January 2025
Department of Molecular Biosciences, University of South Florida, 4202 E Fowler Ave, Tampa, FL, 33620, USA.
Unraveling the signaling roles of intermediate complexes is pivotal for G protein-coupled receptor (GPCR) drug development. Despite hundreds of GPCR-Gαβγ structures, these snapshots primarily capture the fully activated complex. Consequently, the functions of intermediate GPCR-G protein complexes remain elusive.
View Article and Find Full Text PDFACS Chem Neurosci
January 2025
School of Health & Life Sciences, Teesside University, Middlesbrough TS1 3BX, United Kingdom.
The aggregation of α-synuclein is crucial to the development of Lewy body diseases, including Parkinson's disease and dementia with Lewy bodies. The aggregation pathway of α-synuclein typically involves a defined sequence of nucleation, elongation, and secondary nucleation, exhibiting prion-like spreading. This study employed Raman spectroscopy and machine learning analysis, alongside complementary techniques, to characterize the biomolecular changes during the fibrillation of purified recombinant wild-type α-synuclein protein.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
January 2025
IITH: Indian Institute of Technology Hyderabad, Chemistry, Kandi, Sangaredddy, 502285, INDIA.
A squaramide-based monomer, designed for topochemical azide-alkyne cycloaddition (TAAC) polymerization, crystallizes as two polymorphs, M1 and M2, both having crystal packing suitable for topochemical polymerization. The hydrogen-bonding between squaramide units bias the molecular organization in both the polymorphs. 3D packing of H-bonded stacks of monomer lead to juxtaposition of azide and alkyne units of adjacent molecules in a transition-state-like arrangement for their regiospecific cycloaddition reaction.
View Article and Find Full Text PDFBiochemistry
January 2025
Department of Biological Sciences, Indian Institute of Science Education and Research Mohali, Sector 81, SAS Nagar, Manauli, Mohali, Punjab 140306, India.
Listeriolysin O (LLO) is a potent membrane-damaging pore-forming toxin (PFT) secreted by the bacterial pathogen . LLO belongs to the family of cholesterol-dependent cytolysins (CDCs), which specifically target cholesterol-containing cell membranes to form oligomeric pores and induce membrane damage. CDCs, including LLO, harbor designated pore-forming motifs.
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