Dependence of the size of a protein-SDS complex on detergent and Na+ concentrations.
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.
Gangabadage
Chinthaka Sanath
CS
Department of Chemistry, University of Ruhuna, Matara, Sri Lanka, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 5a Pawińskiego, 02-106 Warsaw, Poland.
Najda
Andzelika
A
Bogdan
Diana
D
Wijmenga
Sybren S
SS
Tessari
Marco
M
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*
D036022:Capsid Proteins; D008823:Micelles; D013501:Surface-Active Agents; C025668:coat protein, Bacteriophage M13; D012967:Sodium Dodecyl Sulfate; D012964:Sodium