Cooling a nanomechanical resonator by a triple quantum dot

We propose an approach for achieving ground-state cooling of a nanomechanical resonator (NAMR) capacitively coupled to a triple quantum dot (TQD). This TQD is an electronic analog of a three-level atom in $\Lambda$ configuration which allows an electron to enter it via lower-energy states and to exit only from a higher-energy state. By tuning the degeneracy of the two lower-energy states in the TQD, an electron can be trapped in a dark state caused by destructive quantum interference between the two tunneling pathways to the higher-energy state. Therefore, ground-state cooling of an NAMR can be achieved when electrons absorb readily and repeatedly energy quanta from the NAMR for excitations.Comment: 6 pages, 3 figure

Observable effects of the quantum adiabatic phase for noncyclic evolution

Journal ArticleIt is pointed out that, contrary to naive expectation, the gauge structure or Berry connection recently found in slowly varying quantum systems gives rise to observable effects even for noncyclic evolutions corresponding to open paths in parameter space. We propose to test such effects in muon spin resonance and in level-crossing resonance in muon-spin-rotation spectroscopy. In our proposals either the probe or the system itself has a lifetime much shorter than the period of one adiabatic cycle

F-wave heavy-light meson spectroscopy in QCD sum rules and heavy quark effective theory

We study the F-wave c_bar s heavy meson doublets (2+,3+) and (3+,4+). They have large orbital excitations L=3, and may be good challenges (tests) for theoretical studies. To study them we use the method of QCD sum rule in the framework of heavy quark effective theory. Their masses are predicted to be m_{(2+,3+)} = (3.45 \pm 0.25, 3.50 \pm 0.26) GeV and m_{(3+,4+)} = (3.20 \pm 0.22, 3.26 \pm 0.23) GeV, with mass splittings Delta m_{(2+,3+)} = m_{3+} - m_{2+} = 0.046 \pm 0.030 GeV and Delta m_{(3+,4+)} = 0.053 \pm 0.044 GeV, respectively. We note that this is a pioneering work and these results are provisional.Comment: 10 pages, 8 figures, 3 tables, accepted by PR

Residues Responsible for the Selectivity of α-Conotoxins for Ac-AChBP or nAChRs

Nicotinic acetylcholine receptors (nAChRs) are targets for developing new drugs to treat severe pain, nicotine addiction, Alzheimer disease, epilepsy, etc. α-Conotoxins are biologically and chemically diverse. With 12–19 residues and two disulfides, they can be specifically selected for different nAChRs. Acetylcholine-binding proteins from Aplysia californica (Ac-AChBP) are homologous to the ligand-binding domains of nAChRs and pharmacologically similar. X-ray structures of the α-conotoxin in complex with Ac-AChBP in addition to computer modeling have helped to determine the binding site of the important residues of α-conotoxin and its affinity for nAChR subtypes. Here, we present the various α-conotoxin residues that are selective for Ac-AChBP or nAChRs by comparing the structures of α-conotoxins in complex with Ac-AChBP and by modeling α-conotoxins in complex with nAChRs. The knowledge of these binding sites will assist in the discovery and design of more potent and selective α-conotoxins as drug leads