62 research outputs found

    Process pi p -> pi pi N at high energies and moderate momenta transferred to the nucleon and the determination of parameters of the f_0(980) and f_0(1300)

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    We present the results of simultaneous analysis of the S-wave pi pi-spectra in the reactions pi^- p -> (pi^0 pi^0)_S n at p_{lab}=38 GeV/c (GAMS) and pi^- p -> (pi^+ pi^-)_S n at p_{lab}=18 GeV/c (E852 Collaboration) at moderate momenta transferred to the nucleon, |t| < 1.5 (GeV/c)^2. The t-distributions are described by the reggeized pi- and a_1-exchanges provided by the leading and daughter trajectories, while the M_{pi pi}-spectra are determined by a set of scalar-isoscalar resonances. With M_{pi pi}-distributions averaged over t-intervals, we have found several solutions given by different t-channel exchange mechanisms at |t| ~ (0.5-1.5) (GeV/c)^2, with resonance parameters close to each other. We conclude that despite a poor knowledge of the structure of the t-exchange, the characteristics of resonances such as masses and widths can be reliably determined using the processes under discussion. As to pole positions, we have found (1031 +/- 10) - i(35 +/- 6) MeV for f_0(980) and (1315 +/- 20) - i(150 +/- 30) MeV for f_0(1300).Comment: 17 pages, RevTeX, 10 EPS figures, misprints correcte

    ATP synthase: from single molecule to human bioenergetics

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    ATP synthase (FoF1) consists of an ATP-driven motor (F1) and a H+-driven motor (Fo), which rotate in opposite directions. FoF1 reconstituted into a lipid membrane is capable of ATP synthesis driven by H+ flux. As the basic structures of F1 (α3β3γδε) and Fo (ab2c10) are ubiquitous, stable thermophilic FoF1 (TFoF1) has been used to elucidate molecular mechanisms, while human F1Fo (HF1Fo) has been used to study biomedical significance. Among F1s, only thermophilic F1 (TF1) can be analyzed simultaneously by reconstitution, crystallography, mutagenesis and nanotechnology for torque-driven ATP synthesis using elastic coupling mechanisms. In contrast to the single operon of TFoF1, HFoF1 is encoded by both nuclear DNA with introns and mitochondrial DNA. The regulatory mechanism, tissue specificity and physiopathology of HFoF1 were elucidated by proteomics, RNA interference, cytoplasts and transgenic mice. The ATP synthesized daily by HFoF1 is in the order of tens of kilograms, and is primarily controlled by the brain in response to fluctuations in activity
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