scholarly journals Squark mass determination at the next generation of lineare+e−colliders

1994 ◽  
Vol 49 (5) ◽  
pp. 2369-2381 ◽  
Author(s):  
Jonathan L. Feng ◽  
Donald E. Finnell
2017 ◽  
Vol 14 (S339) ◽  
pp. 22-22
Author(s):  
M. Burleigh

AbstractThis talk introduced and described the Next Generation Transit Survey (NGTS), which is a new ground-based transit survey operating at the ESO Paranal Observatory. NGTS has been designed to achieve better photometric precision than previous ground-based surveys; it aims to detect Neptune-sized planets around Sun-like stars, and sub-Neptunes around M dwarfs that are sufficiently bright for radial-velocity confirmation and mass determination. NGTS is also optimised for ground-based follow up of exoplanet candidates from TESS and PLATO. I presented early results from the survey, and described the status of our HARPS radial-velocity and SAAO photometric follow-ups of exoplanet candidates.


Author(s):  
M. K. Lamvik ◽  
A. V. Crewe

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.


2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska

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.


2004 ◽  
Vol 171 (4S) ◽  
pp. 389-389
Author(s):  
Manoj Monga ◽  
Ramakrishna Venkatesh ◽  
Sara Best ◽  
Caroline D. Ames ◽  
Courtney Lee ◽  
...  

1996 ◽  
Vol 41 (1) ◽  
pp. 52-53
Author(s):  
Lisa C. McGuire
Keyword(s):  

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