arXiv subjects

Jose Luis Alonso

Publications and source records attributed to Jose Luis Alonso.

4 recordsLinked to original sources

arXiv2013

Laboratory and Astronomical Discovery of HydroMagnesium Isocyanide

We report on the detection of hydromagnesium isocyanide, HMgNC, in the laboratory and in the carbon rich evolved star IRC+10216. The J=1-0 and J=2-1 lines were observed in our microwave laboratory equipment in Valladolid with a spectral accuracy of 3\,KHz. The hyperfine structure produced by the Nitrogen atom was resolved for both transitions. The derived rotational constants from the laboratory data are $B_0$=5481.4333(6)\,MHz, $D_0$=2.90(8)\,KHz, and $eQq(N)$=-2.200(2)\,MHz. The predicted frequencies for the rotational transitions of HMgNC in the millimeter domain have an accuracy of 0.2-0.7\,MHz. Four rotational lines of this species, J=8-7, J=10-9, J=12-11 and J=13-12, have been detected towards IRC+10216. The differences between observed and calculated frequencies are $<$0.5\,MHz. The rotational constants derived from space frequencies are $B_0$=5481.49(3)\,MHz and $D_0$=3.2(1)\,KHz, i.e., identical to the laboratory ones. A merged fit to the laboratory and space frequencies provides $B_0$=5481.4336(4)\,MHz and $D_0$=2.94(5)\,KHz. We have derived a column density for HMgNC of (6$\pm$2)$\times10^{11}$\,cm$^{-2}$. From the observed line profiles the molecule have to be produced produced in the layer where other metal-isocyanides have been already found in this source. The abundance ratio between MgNC and its hydrogenated variety, HMgNC, is $\simeq$20.

astro-ph.GA↗

arXiv2005

Relevant distance between two different instances of the same potential energy in protein folding

In the context of complex systems and, particularly, of protein folding, a physically meaningful distance is defined which allows to make useful statistical statements about the way in which energy differences are modified when two different instances of the same potential-energy function are used. When the two instances arise from the fact that different algorithms or different approximations are used, the distance herein defined may be used to evaluate the relative accuracy of the two methods. When the difference is due to a change in the free parameters of which the potential depends on, the distance can be used to quantify, in each region of parameter space, the robustness of the modeling to such a change and this, in turn, may be used to assess the significance of a parameters' fit. Both cases are illustrated with a practical example: the study of the Poisson-based solvation energy in the Trp-Cage protein (PDB code 1L2Y).

q-bio.BM↗

arXiv2004

Do theoretical physicists care about the protein-folding problem?

The prediction of the biologically active native conformation of a protein is one of the fundamental challenges of structural biology. This problem remains yet unsolved mainly due to three factors: the partial knowledge of the effective free energy function that governs the folding process, the enormous size of the conformational space of a protein and, finally, the relatively small differences of energy between conformations, in particular, between the native one and the ones that make up the unfolded state. Herein, we recall the importance of taking into account, in a detailed manner, the many interactions involved in the protein folding problem (such as steric volume exclusion, Ramachandran forces, hydrogen bonds, weakly polar interactions, coulombic energy or hydrophobic attraction) and we propose a strategy to effectively construct a free energy function that, including the effects of the solvent, could be numerically tractable. It must be pointed out that, since the internal free energy function that is mainly described does not include the constraints of the native conformation, it could only help to reach the 'molten globule' state. We also discuss about the limits and the lacks from which suffer the simple models that we, physicists, love so much.

q-bio.BM↗

arXiv1992

The S, U and Δρparameters in the Zaragoza proposal for lattice chiral gauge fermions

Using the Zaragoza proposal for lattice chiral gauge fermions, the S, U and Δρparameters have been calculated at one loop. It is shown that the continuum values for these quantities can be reproduced without requiring explicit fine tuning of counterterms. Furthermore, fermion fields doubling is not necessary. To the best of our knowledge, the Zaragoza proposal is the only scheme which has these properties. A necessary (although not sufficient) symmetry is found to support the calculations. Previous results for some of these parameters in other lattice chiral regularizations are revisited in the light of this symmetry.

hep-lat↗