再生不良性貧血における分子病態の解明と診断・治療のバイオマーカーの開発

第16回　金沢大学十全医学賞受賞論

Direct diagnostics of forming massive stars: stellar pulsation and periodic variability of maser sources

The 6.7 GHz methanol maser emission, a tracer of forming massive stars, sometimes shows enigmatic periodic flux variations over several 10-100 days. In this Letter, we propose that this periodic variations could be explained by the pulsation of massive protostars growing under rapid mass accretion with rates of Mdot > 10^-3 Msun/yr. Our stellar evolution calculations predict that the massive protostars have very large radius exceeding 100 Rsun at maximum, and we here study the pulsational stability of such the bloated protostars by way of the linear stability analysis. We show that the protostar becomes pulsationally unstable with various periods of several 10-100 days, depending on different accretion rates. With the fact that the stellar luminosity when the star is pulsationally unstable also depends on the accretion rate, we derive the period-luminosity relation log (L/Lsun) = 4.62 + 0.98log(P/100 day), which is testable with future observations. Our models further show that the radius and mass of the pulsating massive protostar should also depend on the period. It would be possible to infer such protostellar properties and the accretion rate with the observed period. Measuring the maser periods enables a direct diagnosis of the structure of accreting massive protostars, which are deeply embedded in dense gas and inaccessible with other observations.Comment: 5 pages, 3 figures, 1 table, accepted for publication in ApJ

Precipitant-Free Lysozyme Crystals Grown by Centrifugal Concentration Reveal Structural Changes

The three-dimensional (3D) structure of a protein molecule in its crystal need not correspond to that found in vivo in many cases, since we usually crystallize protein molecules using precipitants (salts, organic solvents, polymeric electrolytes, etc.), and the precipitants are often incorporated into crystals along with the protein molecules. Although precipitant-free crystallization methods would solve these problems, such methods had not yet been established. We have achieved a novel precipitant-free crystallization method by liquid-liquid phase separation during the centrifugal concentration of lysozyme in ultra-pure water. In the 3D structure of the precipitant-free crystal, lysozyme loses a sodium cation and changes the position of Ser 72. Deionization of the solution also appears to induce a change in the position of Asp 101 and an increase in the activity of lysozyme

Betrachtungen zu „Tannhäuser“ unter drei Gesichtspunkten

諸沢巖教授古稀・退職記念、中島巖教授退職記