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Title: Structural study of surfactant-dependent interaction with protein

Small-angle neutron scattering (SANS) has been used to study the complex structure of anionic BSA protein with three different (cationic DTAB, anionic SDS and non-ionic C12E10) surfactants. These systems form very different surfactant-dependent complexes. We show that the structure of protein-surfactant complex is initiated by the site-specific electrostatic interaction between the components, followed by the hydrophobic interaction at high surfactant concentrations. It is also found that hydrophobic interaction is preferred over the electrostatic interaction in deciding the resultant structure of protein-surfactant complexes.
Authors:
;  [1] ;  [2]
  1. Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai 400 085 (India)
  2. Laboratory for Neutron Scattering, Paul Scherrer Institut, CH-5232 PSI Villigen (Switzerland)
Publication Date:
OSTI Identifier:
22490208
Resource Type:
Journal Article
Resource Relation:
Journal Name: AIP Conference Proceedings; Journal Volume: 1665; Journal Issue: 1; Conference: 59. DAE solid state physics symposium 2014, Tamilnadu (India), 16-20 Dec 2014; Other Information: (c) 2015 AIP Publishing LLC; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ABUNDANCE; CONCENTRATION RATIO; ELECTROSTATICS; NEUTRON DIFFRACTION; PROTEINS; SMALL ANGLE SCATTERING; SURFACTANTS