Giant valley-isospin conductance oscillations in ballistic graphene

At high magnetic fields the conductance of graphene is governed by the half-integer quantum Hall effect. By local electrostatic gating a \textit{p-n} junction perpendicular to the graphene edges can be formed, along which quantum Hall channels co-propagate. It has been predicted by Tworzid\l{}o and co-workers that if only the lowest Landau level is filled on both sides of the junction, the conductance is determined by the valley (isospin) polarization at the edges and by the width of the flake. This effect remained hidden so far due to scattering between the channels co-propagating along the \textit{p-n} interface (equilibration). Here we investigate \textit{p-n} junctions in encapsulated graphene with a movable \textit{p-n} interface with which we are able to probe the edge-configuration of graphene flakes. We observe large quantum conductance oscillations on the order of \si{e^2/h} which solely depend on the \textit{p-n} junction position providing the first signature of isospin-defined conductance. Our experiments are underlined by quantum transport calculations.Comment: 5 pages, 4 figure

The Grizzly, March 2, 1993

Airband Raises Over $1300 for Charity • The United States of Europe with Modern Languages • Explosion at World Trade Center • Meistersingers to Tour New England • Flowers of Hope • Senior Profile: Maria Rojas • The Problem With Centrists • Men\u27s Track and Field at MACs • Gymnasts Finish With High Scorehttps://digitalcommons.ursinus.edu/grizzlynews/1311/thumbnail.jp

The Ursinus Weekly, October 22, 1951

Seniors elect Paul Doughty new president • Full day planned for return of Old Timers • Weekly staff is enlarged by new members • Y retreat termed success; Varied program enjoyed • Chem group plans trip to exhibition • Ruby pictures slated • FTA plans roast for all members • Red Cross plans first aid, life saving courses for students • \u2755 show features night club life • 4 members added to Lantern staff • Chairmen named for junior events • Jobs offered • Scientific phenomena featured in magic show October 31 • Y cabinet makes new appointments • F&M demands no pre-game visitation • Editorials: New topics needed; British bar allusions • Letters to the editor • Alumni • Engagement • Identical twins revolt against heredity laws • Cutting classes requires skillful maneuvering and also fat purse • Ruth Reed goes to Venezuela for Y summer work • Ursinus meets Wagner on Homecoming day • Spying by Happy Chandler helped Centre top Harvard • Belles are victors in last 60 seconds as Rittenhouse scores winning goal • Glock paces Ursinus scorers • Curtis takes lead in interdorm loop • Bakermen lose to Rutgers, 5-4 • Grizzlies beat Swarthmore to gain football holiday • Swarthmore defeated in J.V. hockey, 5-4 • Pre-med society changes constitution; Election slated • WSGA secures dates for activities meetings during year • Debating explained • Meistersingers practice • Pre-legal drive opens • Chess club loseshttps://digitalcommons.ursinus.edu/weekly/1524/thumbnail.jp

Structure and function of the metagenomic plastic-degrading polyester hydrolase PHL7 bound to its product

The recently discovered metagenomic-derived polyester hydrolase PHL7 is able to efficiently degrade amorphous polyethylene terephthalate (PET) in post-consumer plastic waste. We present the cocrystal structure of this hydrolase with its hydrolysis product terephthalic acid and elucidate the influence of 17 single mutations on the PET-hydrolytic activity and thermal stability of PHL7. The substrate-binding mode of terephthalic acid is similar to that of the thermophilic polyester hydrolase LCC and deviates from the mesophilic IsPETase. The subsite I modifications L93F and Q95Y, derived from LCC, increased the thermal stability, while exchange of H185S, derived from IsPETase, reduced the stability of PHL7. The subsite II residue H130 is suggested to represent an adaptation for high thermal stability, whereas L210 emerged as the main contributor to the observed high PET-hydrolytic activity. Variant L210T showed significantly higher activity, achieving a degradation rate of 20 µm h−1 with amorphous PET films

The Grizzly, September 29, 1992

Yes, Mom, I Really Do Live Here: Parents Day 1992 • APO and Demas Honored • Taking Time to Talk with New Faculty • How Ursinus Rates • International Wednesday • Literature? At Ursinus? • Spotlight: Milo Winter • Nothing to Do? Then Make Something Happen! • An Alternative to Litigation • Letters to the Editor • An Educated Vote • The Cross-Country Steamroller • Sports Week in Reviewhttps://digitalcommons.ursinus.edu/grizzlynews/1299/thumbnail.jp

The Grizzly, February 23, 1993

Helen Thomas, White House Correspondent Speaks • Pledging: Girls\u27 Results From Fall 1992 Versus Outward Bound, 1993 • Clinton\u27s Plans for Peace • Airband, MTV Here • Evaluating the Curriculum of Ursinus • Ursinus Welcomes Ishmael Reed • Movie Review: Sommersby • South Street: An Informative Perspective • Senior Profile: Casey Price • Who\u27s in Charge at 1600? • Letter to the Editor • Gymnasts Achieve Season-High • Two Ursinus Legends Step Down • Thomas adds Sports Manager Duties • Swimmers Done • Bears Finish 7-17; Look to Bright Futurehttps://digitalcommons.ursinus.edu/grizzlynews/1310/thumbnail.jp

The spatio-temporal organization of mitochondrial F1FO ATP synthase in cristae depends on its activity mode.

F1FO ATP synthase, also known as complex V, is a key enzyme of mitochondrial energy metabolism that can synthesize and hydrolyze ATP. It is not known whether the ATP synthase and ATPase function are correlated with a different spatio-temporal organisation of the enzyme. In order to analyze this, we tracked and localized single ATP synthase molecules in situ using live cell microscopy. Under normal conditions, complex V was mainly restricted to cristae indicated by orthogonal trajectories along the cristae membranes. In addition confined trajectories that are quasi immobile exist. By inhibiting glycolysis with 2-DG, the activity and mobility of complex V was altered. The distinct cristae-related orthogonal trajectories of complex V were obliterated. Moreover, a mobile subpopulation of complex V was found in the inner boundary membrane. The observed changes in the ratio of dimeric/monomeric complex V, respectively less mobile/more mobile complex V and its activity changes were reversible. In IF1-KO cells, in which ATP hydrolysis is not inhibited by IF1, complex V was more mobile, while inhibition of ATP hydrolysis by BMS-199264 reduced the mobility of complex V. Taken together, these data support the existence of different subpopulations of complex V, ATP synthase and ATP hydrolase, the latter with higher mobility and probably not prevailing at the cristae edges. Obviously, complex V reacts quickly and reversibly to metabolic conditions, not only by functional, but also by spatial and structural reorganization.This work was supported by the DFG (INST 190/167-2). K. Busch is associated with the CiM (Cells in Motion cluster, Munster).S

The Grizzly, November 3, 1989

Wismer Woes • Curriculum Changes Affect all Students at U.C. • Letters: A Voice for Love ; Coaching Cowardess • Alcohol Awareness • Club Sails Smoothly • For Nature\u27s Nurture • Bears Struggle with Division I • Honors Galore • X-C Teams Look to MAC\u27s • Hoopla!https://digitalcommons.ursinus.edu/grizzlynews/1245/thumbnail.jp