Protein-protein interactions in ovalbumin solutions studied by small-angle scattering: Effect of ionic strength and the chemical nature of cations

Journal of Physical Chemistry B

Volumn 114, Issue 11, 2010, Pages 3776-3783

  Ianeselli, Luca ^a   Zhang, Fajun ^a   Skoda, Maximilian W A ^b   Jacobs, Robert M J ^c   Martin, Richard A ^d   Callow, Shirley ^e   Prévost, Sylvain ^f   Schreiber, Frank ^a  

^a UNIVERSITY OF TÜBINGEN   (Germany)

^b RUTHERFORD APPLETON LABORATORY   (United Kingdom)

^c UNIVERSITY OF OXFORD   (United Kingdom)

^d ASTON UNIVERSITY   (United Kingdom)

^e EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^f HAHN MEITNER INSTITUT   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

APPROXIMATION THEORY; BODY FLUIDS; PHYSIOLOGICAL MODELS; POSITIVE IONS; PROTEINS; SCATTERING; SODIUM CHLORIDE; YTTRIUM;

BOVINE SERUM ALBUMINS; CHEMICAL NATURE; COULOMBIC INTERACTIONS; EFFECT OF IONIC STRENGTH; EFFECTIVE INTERACTIONS; ELECTROSTATIC REPULSION; FORM FACTORS; GLOBULAR PROTEINS; MONOVALENT SALT; NEGATIVE CHARGE; NEUTRAL PH; OVALBUMINS; PHYSIOLOGICAL CONDITION; PROTEIN SOLUTION; PROTEIN-PROTEIN INTERACTIONS; RE-DISSOLUTION; REENTRANT CONDENSATION; SALT ADDITION; SALT CONCENTRATION; SCATTERING DATA; SCATTERING INTENSITY; SMALL-ANGLE SCATTERING; SMALL-ANGLE X-RAYS; STRUCTURE FACTORS; YTTRIUM CHLORIDE;

IONIC STRENGTH;

EID: 77949805991     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp9112156     Document Type: Article

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