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Phase behavior of lysozyme solutions in the liquid-liquid phase coexistence region at high hydrostatic pressures.
Schulze, Julian; Möller, Johannes; Weine, Jonathan; Julius, Karin; König, Nico; Nase, Julia; Paulus, Michael; Tolan, Metin; Winter, Roland.
Afiliação
  • Schulze J; Fakultät Physik/DELTA, TU Dortmund, D-44221 Dortmund, Germany.
  • Möller J; ESRF - The European Synchrotron, 38043 Grenoble, France.
  • Weine J; Fakultät Physik/DELTA, TU Dortmund, D-44221 Dortmund, Germany.
  • Julius K; Fakultät Physik/DELTA, TU Dortmund, D-44221 Dortmund, Germany.
  • König N; Fakultät Physik/DELTA, TU Dortmund, D-44221 Dortmund, Germany.
  • Nase J; Fakultät Physik/DELTA, TU Dortmund, D-44221 Dortmund, Germany.
  • Paulus M; Fakultät Physik/DELTA, TU Dortmund, D-44221 Dortmund, Germany.
  • Tolan M; Fakultät Physik/DELTA, TU Dortmund, D-44221 Dortmund, Germany.
  • Winter R; Physikalische Chemie, Fakultät für Chemie und Chemische Biologie, TU Dortmund, Otto-Hahn Str. 4a, 44227 Dortmund, Germany. roland.winter@tu-dortmund.de.
Phys Chem Chem Phys ; 18(21): 14252-6, 2016 05 25.
Article em En | MEDLINE | ID: mdl-27165990
ABSTRACT
We present results from small-angle X-ray scattering and turbidity measurements on the effect of high hydrostatic pressure on the phase behavior of dense lysozyme solutions in the liquid-liquid phase separation region, and characterize the underlying intermolecular protein-protein interactions as a function of temperature and pressure under charge-screening conditions (0.5 M NaCl). A reentrant liquid-liquid phase separation region is observed at elevated pressures, which may originate in the pressure dependence of the solvent-mediated protein-protein interaction. A temperature-pressure-concentration phase diagram was constructed for highly concentrated lysozyme solutions over a wide range of temperatures, pressures and protein concentrations including the critical region of the liquid-liquid miscibility gap.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Muramidase Idioma: En Revista: Phys Chem Chem Phys Assunto da revista: BIOFISICA / QUIMICA Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Muramidase Idioma: En Revista: Phys Chem Chem Phys Assunto da revista: BIOFISICA / QUIMICA Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Alemanha