Using adiabatic invariance and the Bohr-Sommerfeld quantization rule we investigate the entropy spectroscopy of two black holes of heterotic string theory,the charged GMGHS and the rotating Sen solutions.It is shown t...Using adiabatic invariance and the Bohr-Sommerfeld quantization rule we investigate the entropy spectroscopy of two black holes of heterotic string theory,the charged GMGHS and the rotating Sen solutions.It is shown that the entropy spectrum is equally spaced in both cases,identically to the spectrum obtained before for Schwarzschild,Reissner-Nordstr？m and Kerr black holes.Since the adiabatic invariance method does not use quasinormal mode analysis,there is no need to impose the small charge or small angular momentum limits and there is no confusion on whether the real part or the imaginary part of the modes is responsible for the entropy spectrum.展开更多
NMR spectroscopy and X-ray crystallography are two premium methods for determining the atomic structures of macro-biomolecular complexes.Each method has unique strengths and weaknesses.While the two techniques are hig...NMR spectroscopy and X-ray crystallography are two premium methods for determining the atomic structures of macro-biomolecular complexes.Each method has unique strengths and weaknesses.While the two techniques are highly complementary,they have generally been used separately to address the structure and functions of biomolecular complexes.In this review,we emphasize that the combination of NMR spectroscopy and X-ray crystallography offers unique power for elucidating the structures of complicated protein assemblies.We demonstrate,using several recent examples from our own laboratory,that the exquisite sensitivity of NMR spectroscopy in detecting the conformational properties of individual atoms in proteins and their complexes,without any prior knowledge of conformation,is highly valuable for obtaining the high quality crystals necessary for structure determination by X-ray crystallography.Thus NMR spectroscopy,in addition to answering many unique structural biology questions that can be addressed specifically by that technique,can be exceedingly powerful in modern structural biology when combined with other techniques including X-ray crystallography and cryo-electron microscopy.展开更多
基金Supported by the Universidad Nacional de Colombia. Hermes Project Code 13038
文摘Using adiabatic invariance and the Bohr-Sommerfeld quantization rule we investigate the entropy spectroscopy of two black holes of heterotic string theory,the charged GMGHS and the rotating Sen solutions.It is shown that the entropy spectrum is equally spaced in both cases,identically to the spectrum obtained before for Schwarzschild,Reissner-Nordstr？m and Kerr black holes.Since the adiabatic invariance method does not use quasinormal mode analysis,there is no need to impose the small charge or small angular momentum limits and there is no confusion on whether the real part or the imaginary part of the modes is responsible for the entropy spectrum.
基金supported by grants from the Research Grants Council of Hong Kong to M.Z.supported by the National Major Basic Research Program of China (Grant No. 2011CB910500)+3 种基金the National Natural Science Foundation of China (Grant No. 31070657)the Knowledge Innovation Program of the Chinese Academy of Sciences (Grant No. KSCX2-YW-R-154)The NMR spectrometers used in our studies were funded by donations from the Hong Kong Jockey Club Charity Foundationthe Special Equipment Grant from RGC of Hong Kong (Grant No. SEG_HKUST06)
文摘NMR spectroscopy and X-ray crystallography are two premium methods for determining the atomic structures of macro-biomolecular complexes.Each method has unique strengths and weaknesses.While the two techniques are highly complementary,they have generally been used separately to address the structure and functions of biomolecular complexes.In this review,we emphasize that the combination of NMR spectroscopy and X-ray crystallography offers unique power for elucidating the structures of complicated protein assemblies.We demonstrate,using several recent examples from our own laboratory,that the exquisite sensitivity of NMR spectroscopy in detecting the conformational properties of individual atoms in proteins and their complexes,without any prior knowledge of conformation,is highly valuable for obtaining the high quality crystals necessary for structure determination by X-ray crystallography.Thus NMR spectroscopy,in addition to answering many unique structural biology questions that can be addressed specifically by that technique,can be exceedingly powerful in modern structural biology when combined with other techniques including X-ray crystallography and cryo-electron microscopy.
