The nucleon mass in N_f=2 lattice QCD: finite size effects from chiral perturbation theory

In the framework of relativistic SU(2)_f baryon chiral perturbation theory we calculate the volume dependence of the nucleon mass up to and including O(p^4). Since the parameters in the resulting finite size formulae are fixed from the pion mass dependence of the large volume nucleon masses and from phenomenology, we obtain a parameter-free prediction of the finite size effects. We present mass data from the recent N_f=2 simulations of the UKQCD and QCDSF collaborations and compare these data as well as published mass values from the dynamical simulations of the CP-PACS and JLQCD collaborations with the theoretical expectations. Remarkable agreement between the lattice data and the predictions of chiral perturbation theory in a finite volume is found.Comment: 23 pages, 5 figures; references added + minor corrections; one more reference added, typo in eq.(25) corrected, additional clarifying remark

Axial and tensor charge of the nucleon with dynamical fermions

We present preliminary results for the axial and tensor charge of the nucleon obtained from simulations with N_f=2 clover fermions. A comparison with chiral perturbation theory is attempted.Comment: Talk presented at Lattice2004(weak), Fermilab, June 21-26, 2004, 3 pages, 3 figures, v2: one reference added, v3: acknowledgement extende

The axial charge of the nucleon on the lattice and in chiral perturbation theory

We present recent Monte Carlo data for the axial charge of the nucleon obtained by the QCDSF-UKQCD collaboration for N_f=2 dynamical quarks. We compare them with formulae from chiral perturbation theory in finite and infinite volume and find a remarkably consistent picture.Comment: 6 pages, 3 figures, talk presented at Lattice2005 (weak matrix elements), needs PoS.cl

Comparison of the structure and activity of glycosylated and asglycosylated human carboxylesterase 1

Human Carboxylesterase 1 (hCES1) is the key liver microsomal enzyme responsible for detoxification and metabolism of a variety of clinical drugs. To analyse the role of the single N-linked glycan on the structure and activity of the enzyme, authentically glycosylated and aglycosylated hCES1, generated by mutating asparagine 79 to glutamine, were produced in human embryonic kidney cells. Purified enzymes were shown to be predominantly trimeric in solution by analytical ultracentrifugation. The purified aglycosylated enzyme was found to be more active than glycosylated hCES1 and analysis of enzyme kinetics revealed that both enzymes exhibit positive cooperativity. Crystal structures of hCES1 a catalytically inactive mutant (S221A) and the aglycosylated enzyme were determined in the absence of any ligand or substrate to high resolutions (1.86 Å, 1.48 Å and 2.01 Å, respectively). Superposition of all three structures showed only minor conformational differences with a root mean square deviations of around 0.5 Å over all Cα positions. Comparison of the active sites of these un-liganded enzymes with the structures of hCES1-ligand complexes showed that side-chains of the catalytic triad were pre-disposed for substrate binding. Overall the results indicate that preventing N-glycosylation of hCES1 does not significantly affect the structure or activity of the enzyme