Higher derivative corrections to black hole thermodynamics from supersymmetric matrix quantum mechanics

We perform a direct test of the gauge-gravity duality associated with the system of N D0-branes in type IIA superstring theory at finite temperature. Based on the fact that higher derivative corrections to the type IIA supergravity action start at the order of \alpha'^3, we derive the internal energy in expansion around infinite 't Hooft coupling up to the subleading term with one unknown coefficient. The power of the subleading term is shown to be nicely reproduced by the Monte Carlo data obtained nonperturbatively on the gauge theory side at finite but large effective (dimensionless) 't Hooft coupling constant. This suggests, in particular, that the open strings attached to the D0-branes provide the microscopic origin of the black hole thermodynamics of the dual geometry including \alpha' corrections. The coefficient of the subleading term extracted from the fit to the Monte Carlo data provides a prediction for the gravity side, which can be checked once the complete form of the O(\alpha'^3) corrections to the supergravity action is obtained.Comment: REVTeX4, 4 pages, 2 figures. Ver.2:intuitive derivation of the subleading term adde

Solution structure of the DNA-binding domain of human telomeric protein, hTRF1

AbstractBackground: Mammalian telomeres consist of long tandem arrays of the double-stranded TTAGGG sequence motif packaged by a telomere repeat binding factor, TRF1. The DNA-binding domain of TRF1 shows sequence homology to each of three tandem repeats of the DNA-binding domain of the transcriptional activator c-Myb. The isolated c-Myb-like domain of human TRF1 (hTRF1) binds specifically to telomeric DNA as a monomer, in a similar manner to that of homeodomains. So far, the only three-dimensional structure of a telomeric protein to be determined is that of a yeast telomeric protein, Rap1p. The DNA-binding domain of Rap1p contains two subdomains that are structurally closely related to c-Myb repeats. We set out to determine the solution structure of the DNA-binding domain of hTRF1 in order to establish its mode of DNA binding.Results: The solution structure of the DNA-binding domain of hTRF1 has been determined and shown to comprise three helices. The architecture of the three helices is very similar to that of each Rap1p subdomain and also to that of each c-Myb repeat. The second and third helix form a helix-turn-helix (HTH) variant. The length of the third helix of hTRF1 is similar to that of the second subdomain of Rap1p.Conclusions: The hTRF1 DNA-binding domain is likely to bind to DNA in a similar manner to that of the second subdomain of Rap1p. On the basis of the Rap1p–DNA complex, a model of the hTRF1 DNA-binding domain in complex with human telomeric DNA was constructed. In addition to DNA recognition by the HTH variant, a flexible N-terminal arm of hTRF1 is likely to interact with DNA

Right ventricular function evaluated by volumetric analysis during left heart bypass in a canine model of postischemic cardiac dysfunction

AbstractRight ventricular function during left heart bypass was evaluated by volumetric analysis with a conductance catheter in 12 dogs with postischemic cardiac dysfunction. The conductance catheter was used to assess the volumetric status of the right ventricle and thereby allowed a right ventricular pressure-volume curve to be obtained, in which transient volume loading on the right ventricle was applied. The following right ventricular properties during left heart bypass were assessed and compared with properties measured without left heart bypass, by means of load-independent parameters: maximum elastance, stroke work/end-diastolic volume relation, end-diastolic pressure/volume relation, and stroke work/end-diastolic pressure relation. The stroke volume derived from the conductance catheter and the electromagnetic flow probe showed good linear correlation (r2 = 0.733 to 0.975). After initiation of left heart bypass, maximum elastance did not change significantly, although volume intercept significantly increased, from 1.2 ± 7.3 to 3.6 ± 7.9 ml ( p < 0.05). End-diastolic pressure/volume relation was well fitted to the exponential curve (EDP = e (k1 · EDV+k2) ) and was shifted to the right and downward during left heart bypass; the slope k1 significantly decreased, from 0.12 ± 0.06 to 0.10 ± 0.07 ( p < 0.01). Stroke work/end-diastolic volume relation and stroke work/end-diastolic pressure relation were closely fitted to the linear regression, and their slopes were significantly increased during left heart bypass, from 0.14 ± 0.08 to 0.18 ± 0.08 ( p < 0.05) and from 0.22 ± 0.15 to 0.34 ± 0.19 ( p < 0.01), respectively. These results suggest that the decompression of the left ventricle and septal shifting by left heart bypass provide good diastolic compliance and good systolic performance because of afterload unloading of the right ventricle. Thus the left heart bypass improved the overall right ventricular performance, particularly at higher end-diastolic pressures, in dogs with postischemic cardiac dysfunction. (J THORAC CARDIOVASC SURG 1995;109:796-803

Location of phosphorylation site and DNA-binding site of a positive regulator, OmpR, involved in activation of the osmoregulatory genes of Escherichia coli

AbstractThe OmpR protein of Escherichia coli is a positive regulator involved in activation of the ompF and ompC genes which encode the major outer membrane proteins OmpF and OmpC, respectively. By employing recombinant DNA techniques, we isolated the N- and C-terminal halves of the OmpR molecule. From the results of biochemical analyses of these fragments, it was concluded that the N-terminal portion contains a site involved in phosphorylation by an OmpR-specific protein kinase EnvZ, whereas the C-terminal part possesses a DNA-binding site for the ompC and ompF promoters

Ground-state properties of neutron-rich Mg isotopes

We analyze recently-measured total reaction cross sections for 24-38Mg isotopes incident on 12C targets at 240 MeV/nucleon by using the folding model and antisymmetrized molecular dynamics(AMD). The folding model well reproduces the measured reaction cross sections, when the projectile densities are evaluated by the deformed Woods-Saxon (def-WS) model with AMD deformation. Matter radii of 24-38Mg are then deduced from the measured reaction cross sections by fine-tuning the parameters of the def-WS model. The deduced matter radii are largely enhanced by nuclear deformation. Fully-microscopic AMD calculations with no free parameter well reproduce the deduced matter radii for 24-36Mg, but still considerably underestimate them for 37,38Mg. The large matter radii suggest that 37,38Mg are candidates for deformed halo nucleus. AMD also reproduces other existing measured ground-state properties (spin-parity, total binding energy, and one-neutron separation energy) of Mg isotopes. Neutron-number (N) dependence of deformation parameter is predicted by AMD. Large deformation is seen from 31Mg with N = 19 to a drip-line nucleus 40Mg with N = 28, indicating that both the N = 20 and 28 magicities disappear. N dependence of neutron skin thickness is also predicted by AMD.Comment: 15 pages, 13 figures, to be published in Phys. Rev.