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Träfflista för sökning "WFRF:(Hübner A.) srt2:(2001-2004)"

Sökning: WFRF:(Hübner A.) > (2001-2004)

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  • Escudero-Pascual, A., et al. (författare)
  • Privacy for location data in mobile networks, a summary
  • 2003
  • Konferensbidrag (refereegranskat)abstract
    • EU Directive 2002/58/EC has introduced, by means of Art. 9, special protection for location data other than traffic data. In this paper, we argue that also location data within traffic data can contain sensitive information about the relative positioning and co-located displacements of mobile nodes and thus alsorequires special protection.Brief discussions are given to how mobility is supported in IP networks, to the level of privacy protection for location data that was introduced in the new European Union data protection directive, and to means of protecting privacy by technology. The concept of \textit{co-located displacements inMobileIP} is introduced and we show how the home agent will be able to determine whether or not a set of mobile nodes move in a co-located fashion.Finally we present how, also for location information within traffic data, privacy-enhancing technologies can be used to provide the level of privacy protection that is required by Art. 9 of the EU Directive 2002/58/EC for location data other than traffic data.
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  • Hubner, Isaac A, et al. (författare)
  • Simulation, experiment, and evolution: Understanding nucleation in protein S6 folding
  • 2004
  • Ingår i: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. - : Proceedings of the National Academy of Sciences. - 0027-8424. ; 101:22, s. 8354-9
  • Tidskriftsartikel (refereegranskat)abstract
    • In this study, we explore nucleation and the transition state ensemble of the ribosomal protein S6 using a Monte Carlo (MC) Go model in conjunction with restraints from experiment. The results are analyzed in the context of extensive experimental and evolutionary data. The roles of individual residues in the folding nucleus are identified, and the order of events in the S6 folding mechanism is explored in detail. Interpretation of our results agrees with, and extends the utility of, experiments that shift -values by modulating denaturant concentration and presents strong evidence for the realism of the mechanistic details in our MC Go model and the structural interpretation of experimental -values. We also observe plasticity in the contacts of the hydrophobic core that support the specific nucleus. For S6, which binds to RNA and protein after folding, this plasticity may result from the conformational flexibility required to achieve biological function. These results present a theoretical and conceptual picture that is relevant in understanding the mechanism of nucleation in protein folding.
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