1. Dependence of the size of a protein-SDS complex on detergent and Na+ concentrations.
- Author
-
Gangabadage CS, Najda A, Bogdan D, Wijmenga SS, and Tessari M
- Subjects
- Micelles, Nuclear Magnetic Resonance, Biomolecular, Particle Size, Capsid Proteins chemistry, Sodium chemistry, Sodium Dodecyl Sulfate chemistry, Surface-Active Agents chemistry
- 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.
- Published
- 2008
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