Contrast analysis of the composition of ribosomes extracted with different purification procedures (Articolo in rivista)

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  • Contrast analysis of the composition of ribosomes extracted with different purification procedures (Articolo in rivista) (literal)
Anno
  • 2000-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1107/S0021889800006300 (literal)
Alternative label
  • Briganti, G; Giordano, R; Londei, P; Valle, F (2000)
    Contrast analysis of the composition of ribosomes extracted with different purification procedures
    in Journal of applied crystallography; WILEY-BLACKWELL PUBLISHING, INC, MALDEN (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Briganti, G; Giordano, R; Londei, P; Valle, F (literal)
Pagina inizio
  • 1113 (literal)
Pagina fine
  • 1118 (literal)
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  • 33 (literal)
Rivista
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  • 6 (literal)
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  • 4 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • [ 1 ] Univ Roma La Sapienza, Dept Phys, INFM, I-00185 Rome, Italy [ 2 ] Dept Phys Messina, INFM, I-98166 Messina, Italy [ 3 ] Univ Bari, Inst Gen Biol, Bari, Italy [ 4 ] Univ Roma La Sapienza, Policlin Umberto I, Dept Cellular Biotechnol & Hematol, I-00185 Rome, Italy [ 5 ] Univ Lausanne, BSP, Inst Condensed Matter Phys, CH-1015 Lausanne, Switzerland (literal)
Titolo
  • Contrast analysis of the composition of ribosomes extracted with different purification procedures (literal)
Abstract
  • The composition and hydration of E. coli ribosomes isolated with different purification protocols has been analysed by combining two experimental techniques: measurements of small-angle neutron scattering (SANS), for two different isotopic solvent compositions, and refractive index (RI) increments. From the contrast between the solvent and solute scattering densities and the molar polarizability, determined experimentally with SANS and RI measurements, three independent equations are obtained and three unknown quantities are determined: (i) the volume of the solute hydrated skeleton Vs, (ii) the material contained in it, namely the biological components, intrinsic (rRNA and proteins) and extrinsic, such as aminoacylsynthetase and elongation factors, (iii) the number of water molecules structurally bound to the ribosome and nonexchangeable with the solvent. From the form factor at infinite contrast, a second definition of the solute volume is obtained, V(s)(c), which represents the volume within the contour surface of the ribosome. This value is generally larger than Vs and can include a certain amount of water molecules, i.e. those inside the volume (V(s)(c)-V(s)). Considering the molar volume of this water to be equal to that of the bulk water, it is possible to evaluate its amount. The particle density calculated from the ribosome components in V(s)(c), including proteins, RNA, bound and unbound water molecules, corresponds to the buoyant density measured for E. coli 70S particles. The two ribosomal preparations display different performances in protein synthesis; hence the results indicate that the optimal condition corresponds to a wider skeleton and contour volume but containing a smaller amount of segregated water molecules. It is believed that the method provides a reliable technique to determine the composition of ribosomes under various experimental conditions (literal)
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