Phase diagram of an exactly solvable t-J ladder model

We study a system of one-dimensional t-J models coupled to a ladder system. A special choice of the interaction between neighbouring rungs leads to an integrable model with supersymmetry, which is broken by the presence of rung interactions. We analyze the spectrum of low-lying excitations and ground state phase diagram at zero temperature.Comment: LaTeX, 8 pp. incl. 1 figur

Phase diagram of the su(8) quantum spin tube

We calculate the phase diagram of an integrable anisotropic 3-leg quantum spin tube connected to the su(8) algebra. We find several quantum phase transitions for antiferromagnetic rung couplings. Their locations are calculated exactly from the Bethe Ansatz solution and we discuss the nature of each of the different phases.Comment: 10 pages, RevTeX, 1 postscript figur

The active form of quinol-dependent Nitric Oxide reductase (qNOR) from Neisseria meningitidis is a dimer

Neisseria meningitidis is carried by nearly a billion humans, causing developmental impairment and over 100 000 deaths a year. A quinol-dependent nitric oxide reductase (qNOR) plays a critical role in the survival of the bacterium in the human host. X-ray crystallographic analyses of qNOR, including that from N. meningitidis (NmqNOR) reported here at 3.15 Å resolution, show monomeric assemblies, despite the more active dimeric sample being used for crystallization. Cryo-electron microscopic analysis of the same chromatographic fraction of NmqNOR, however, revealed a dimeric assembly at 3.06 Å resolution. It is shown that zinc (which is used in crystallization) binding near the dimer-stabilizing TMII region contributes to the disruption of the dimer. A similar destabilization is observed in the monomeric (∼85 kDa) cryo-EM structure of a mutant (Glu494Ala) qNOR from the opportunistic pathogen Alcaligenes (Achromobacter) xylosoxidans, which primarily migrates as a monomer. The monomer–dimer transition of qNORs seen in the cryo-EM and crystallographic structures has wider implications for structural studies of multimeric membrane proteins. X-ray crystallographic and cryo-EM structural analyses have been performed on the same chromatographic fraction of NmqNOR to high resolution. This represents one of the first examples in which the two approaches have been used to reveal a monomeric assembly in crystallo and a dimeric assembly in vitrified cryo-EM grids. A number of factors have been identified that may trigger the destabilization of helices that are necessary to preserve the integrity of the dimer. These include zinc binding near the entry of the putative proton-transfer channel and the preservation of the conformational integrity of the active site. The mutation near the active site results in disruption of the active site, causing an additional destabilization of helices (TMIX and TMX) that flank the proton-transfer channel helices, creating an inert monomeric enzyme

Note on the thermodynamic Bethe Ansatz approach to the quantum phase diagram of the strong coupling ladder compounds

We investigate the low-temperature phase diagram of the exactly solved su(4) two-leg spin ladder as a function of the rung coupling $J_{\perp}$ and magnetic field $H$ by means of the thermodynamic Bethe Ansatz (TBA). In the absence of a magnetic field the model exhibits three quantum phases, while in the presence of a strong magnetic field there is no singlet ground state for ferromagnetic rung coupling. For antiferromagnetic rung coupling, there is a gapped phase in the regime H H_{c2} and a Luttinger liquid magnetic phase in the regime H_{c1} < H < H_{c2}. The critical behaviour derived using the TBA is consistent with the existing experimental, numerical and perturbative results for the strong coupling ladder compounds. This includes the spin excitation gap and the critical fields H_{c1} and H_{c2}, which are in excellent agreement with the experimental values for the known strong coupling ladder compounds (5IAP)_2CuBr_4 2H_2 O, Cu_2(C_5 H_{12} N_2)_2 Cl_4 and (C_5 H_{12} N)_2 CuBr_4. In addition we predict the spin gap $\Delta \approx J_{\perp}-{1/2}J_{\parallel}$ for the weak coupling compounds with $J_{\perp} \sim J_{\parallel}$, such as (VO)_2 P_2 O_7, and also show that the gap opens for arbitrary $J_{\perp}/ J_{\parallel}$.Comment: 10 pages, 3 figure

Staggered Anisotropy Parameter Modification of the Anisotropic t−Jt-J Model

The anisotropic t-J model ($U_q(gl(2|1))$ Perk-Schultz model) with staggered disposition of the anisotropy parameter along a chain is considered and the corresponding ladder type integrable model is constructed. This is a generalisation to spin-1 case of the staggered $XXZ$ spin-1/2 model considered earlier. The corresponding Hamiltonian is calculated and, since it contains next to nearest neighbour interaction terms, can be written in a zig-zag form. The Algebraic Bethe Ansatz technique is applied and the eigenstates, along with eigenvalues of the transfer matrix of the model are found.Comment: 21 pages, Latex2e with amsfonts packag

A new type of lectin discovered in a fish, flathead (Platycephalus indicus), suggests an alternative functional role for mammalian plasma kallikrein*

A skin mucus lectin exhibiting a homodimeric structure and an S–S bond between subunits of ∼40 kDa was purified from flathead Platycephalus indicus (Scorpaeniformes). This lectin, named FHL (FlatHead Lectin), exhibited mannose-specific activity in a Ca2+-dependent manner. Although FHL showed no homology to any previously reported lectins, it did exhibit ∼20% identity to previously discovered plasma kallikreins and coagulation factor XIs of mammals and Xenopus laevis. These known proteins are serine proteases and play pivotal roles in the kinin-generating system or the blood coagulation pathway. However, alignment analysis revealed that while FHL lacked a serine protease domain, it was homologous to the heavy-chain domain of plasma kallikreins and coagulation factor XI therefore suggesting that FHL is not an enzyme but rather a novel animal lectin. On the basis of this finding, we investigated the lectin activity of human plasma kallikrein and revealed that it could indeed act as a lectin. Other genes homologous to FHL were also found in the genome databases of some fish species, but not in mammals. In contrast, plasma kallikreins and coagulation factor XI have yet to be identified in fish. The present findings suggest that these mammalian enzymes may have originally emerged as a lectin and may have evolved into molecules with protease activity after separation from common ancestors