Do clusters contain a large population of dwarf galaxies?

We analyze systematic effects in the determination of the galaxy luminosity function in clusters using a deep mock catalogue constructed from a numerical simulation of a hierarchical universe. The results indicate a strong tendency to derive a rising faint end (\alpha \lsim -1.5) in clusters selected in two dimensions, using a galaxy catalogue constructed with a universal flat luminosity function with $\alpha \simeq -1.0$. This is due to the projection effects inherent in catalogues of clusters constructed using 2 dimensional data. Many of the clusters found in 2d have no significant 3d counterparts, and most suffer from massive background contamination that cannot be corrected for by subtracting random offset fields. The luminosity function of high surface brightness galaxies in the field and within small groups follows a Schechter function with a fairly flat faint end slope, $n(L)\propto L^{\alpha}$ with $\alpha = -0.9$ to -1.2. On the contrary, observational studies of clusters constructed using Abell, EDCC and APM catalogues are systematically found to have steeper luminosity functions with $\alpha = -1.4$ to -2.0. This may be attributed to projection effects rather than a dominant population of high surface brightness dwarf galaxies (M\gsim M^*+2) in clusters. It should be straighforward to confirm our results by measuring redshifts of these faint cluster galaxies.Comment: 23 pages, 7 Postscript figures TeX, accepted for publication in the Astrophysical Journal, e-mail:[email protected] http://iate.oac.uncor.edu/cv.htm

Evaluating the effect of mutations and ligand binding on transthyretin homotetramer dynamics

<div><p>Native transthyretin (TTR) homotetramer dissociation is the first step of the fibrils formation process in amyloid disease. A large number of specific point mutations that destabilize TTR quaternary structure have shown pro-amyloidogenic effects. Besides, several compounds have been proposed as drugs in the therapy of TTR amyloidosis due to their TTR tetramer binding affinities, and therefore, contribution to its integrity. In the present paper we have explored key positions sustaining TTR tetramer dynamical stability. We have identified positions whose mutations alter the most the TTR tetramer equilibrium dynamics based on normal mode analysis and their response to local perturbations. We have found that these positions are mostly localized at β-strands E and F and EF-loop. The monomer-monomer interface is pointed out as one of the most vulnerable regions to mutations that lead to significant changes in the TTR-tetramer equilibrium dynamics and, therefore, induces TTR amyloidosis. Besides, we have found that mutations on residues localized at the dimer-dimer interface and/or at the T4 hormone binding site destabilize the tetramer more than the average. Finally, we were able to compare several compounds according to their effect on vibrations associated to the ligand binding. Our ligand comparison is discussed and analyzed in terms of parameters and measurements associated to TTR-ligand binding affinities and the stabilization of its native state.</p></div