Charm mass determination from QCD charmonium sum rules at order $ \alpha_s^3 $

We use a new compilation of the hadronic RR-ratio from available data for the process e^+e^-\toe+e−→ hadrons below the charm mass to determine the strong coupling \alpha_sαs, using finite-energy sum rules. Quoting our results at the \tauτ mass to facilitate comparison to the results obtained from similar analyses of hadronic \tauτ-decay data, we find \alpha_s(m_\tau^2)=0.298\pm 0.016\pm 0.006αs(mτ2)=0.298±0.016±0.006 in fixed-order perturbation theory, and \alpha_s(m_\tau^2)=0.304\pm 0.018\pm 0.006αs(mτ2)=0.304±0.018±0.006 in contour-improved perturbation theory, where the first error is statistical, and the second error combines various systematic effects. These values are in good agreement with a recent determination from the OPAL and ALEPH data for hadronic \tauτ decays. We briefly compare the R(s)R(s)-based analysis with the \tauτ-based analysis.

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Bottom quark mass determination from low-n sum rules

Nuclear Physics B - Proceedings Supplements ◽

10.1016/j.nuclphysbps.2004.04.162 ◽

2004 ◽

Vol 133 ◽

pp. 186-189 ◽

Cited By ~ 2

Author(s):

G. Corcella ◽

A.H. Hoang

Keyword(s):

Quark Mass ◽

Sum Rules ◽

Bottom Quark ◽

Mass Determination

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MS charm mass from charmonium sum rules with contour improvement

Physics Letters B ◽

10.1016/j.physletb.2004.04.080 ◽

2004 ◽

Vol 594 (1-2) ◽

pp. 127-134 ◽

Cited By ~ 26

Author(s):

A.H. Hoang ◽

M. Jamin

Keyword(s):

Sum Rules ◽

Charm Mass

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A Perturbation Theory for the Population of Atomic Energy Levels in Non-Lte Plasmas

International Astronomical Union Colloquium ◽

10.1017/s025292110010805x ◽

1988 ◽

Vol 102 ◽

pp. 343-347

Author(s):

M. Klapisch

Keyword(s):

Perturbation Theory ◽

Small Parameter ◽

Classification Scheme ◽

Sum Rules ◽

Energy Levels ◽

Natural Classification ◽

Quantum Numbers ◽

Formal Expansion ◽

Atomic Energy Levels ◽

As Effects

AbstractA formal expansion of the CRM in powers of a small parameter is presented. The terms of the expansion are products of matrices. Inverses are interpreted as effects of cascades.It will be shown that this allows for the separation of the different contributions to the populations, thus providing a natural classification scheme for processes involving atoms in plasmas. Sum rules can be formulated, allowing the population of the levels, in some simple cases, to be related in a transparent way to the quantum numbers.

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Mass Determination by Direct Measurement of Electron Scattering

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100114827 ◽

1975 ◽

Vol 33 ◽

pp. 240-241

Author(s):

M. K. Lamvik ◽

A. V. Crewe

Keyword(s):

Cross Section ◽

Electron Scattering ◽

Mass Density ◽

Variable Mass ◽

Scattering Cross Section ◽

Mass Determination ◽

Number Density ◽

Cross Sectional ◽

Thin Slice ◽

Scattering Cross

If a molecule or atom of material has molecular weight A, the number density of such units is given by n=Nρ/A, where N is Avogadro's number and ρ is the mass density of the material. The amount of scattering from each unit can be written by assigning an imaginary cross-sectional area σ to each unit. If the current I0 is incident on a thin slice of material of thickness z and the current I remains unscattered, then the scattering cross-section σ is defined by I=IOnσz. For a specimen that is not thin, the definition must be applied to each imaginary thin slice and the result I/I0 =exp(-nσz) is obtained by integrating over the whole thickness. It is useful to separate the variable mass-thickness w=ρz from the other factors to yield I/I0 =exp(-sw), where s=Nσ/A is the scattering cross-section per unit mass.

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The challenge of detecting modifications on proteins

Essays in Biochemistry ◽

10.1042/ebc20190055 ◽

2020 ◽

Vol 64 (1) ◽

pp. 135-153 ◽

Cited By ~ 1

Author(s):

Lauren Elizabeth Smith ◽

Adelina Rogowska-Wrzesinska

Keyword(s):

Mass Spectrometry ◽

Protein Function ◽

Chemical Properties ◽

Lysine Acetylation ◽

Mass Determination ◽

Post Translational Modifications ◽

Site Specific ◽

The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

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