Autori: Chinthaka Sanath Gangabadage, Andzelika Najda, Diana Bogdan, Sybren S Wijmenga, Marco Tessari
Editorial: J Phys Chem B, 112(14), p.4242-4245, 2008.
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. 15N 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.
Cuvinte cheie: NMR, membrane proteins, SDS, micellar aggregates, protein-SDS complex