Conformational freedom of proteins and the maximal probability of sets of orientations (Articolo in rivista)

Type
Label
  • Conformational freedom of proteins and the maximal probability of sets of orientations (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1088/0266-5611/26/3/035003 (literal)
Alternative label
  • Sgheri L. (2010)
    Conformational freedom of proteins and the maximal probability of sets of orientations
    in Inverse problems (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Sgheri L. (literal)
Pagina inizio
  • 035003-1 (literal)
Pagina fine
  • 035003-19 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 26 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 3 (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • IAC-CNR Sede di Firenze, Via Madonna del Piano 10, 50019 Sesto Fiorentino (FI), Italia (literal)
Titolo
  • Conformational freedom of proteins and the maximal probability of sets of orientations (literal)
Abstract
  • We study the inverse problem of determining the relative orientations of the moving C- and N-terminal domains in a flexible protein from measurements of its mean magnetic susceptibility tensor ?¯ . The latter is an integral average of rotations of the corresponding magnetic susceptibility tensor ?. The largest fraction of time that the two terminals can stay in a given orientation, still producing the ?¯ measurements, is the maximal probability of that orientation. We extend this definition to any measurable subset of the rotation group. This extension permits a quantitative assessment of the results when the generating distribution is either continuous or discrete. We establish some properties of the maximal probability and present some numerical experiments. (literal)
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