title: Dependence of the size of a protein-SDS complex on detergent and Na+ concentrations.
abstract: Sodium dodecyl sulfate (SDS) micelles provide ideal mimetic media for high-resolution NMR studies of membrane proteins and proteins or peptides interacting with micellar aggregates. (15)N NMR relaxation of the backbone amides of a protein-SDS complex has been measured under different experimental conditions. The rotational diffusion time of this complex has been found highly sensitive to detergent and NaCl concentrations. A comparison with calculated rotational diffusion times of protein-free SDS micelles under the same conditions suggests that the size of both aggregates must follow a similar functional dependence on detergent/NaCl concentration.
authors.affiliation: Department of Chemistry, University of Ruhuna, Matara, Sri Lanka, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 5a Pawińskiego, 02-106 Warsaw, Poland.
authors.forename: Chinthaka Sanath
authors.initials: CS
authors.lastname: Gangabadage
authors.forename: Andzelika
authors.initials: A
authors.lastname: Najda
authors.forename: Diana
authors.initials: D
authors.lastname: Bogdan
authors.forename: Sybren S
authors.initials: SS
authors.lastname: Wijmenga
authors.forename: Marco
authors.initials: M
authors.lastname: Tessari
mesh_terms: D036022:Capsid Proteins / Q000737:chemistry*; D008823:Micelles; D019906:Nuclear Magnetic Resonance, Biomolecular; D010316:Particle Size; D012964:Sodium / Q000737:chemistry*; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry*; D013501:Surface-Active Agents / Q000737:chemistry*
chemical_list: D036022:Capsid Proteins; D008823:Micelles; D013501:Surface-Active Agents; C025668:coat protein, Bacteriophage M13; D012967:Sodium Dodecyl Sulfate; D012964:Sodium