Dependence of the size of a protein-SDS complex on detergent and Na+ concentrations |
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Authors: | Gangabadage Chinthaka Sanath Najda Andzelika Bogdan Diana Wijmenga Sybren S Tessari Marco |
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Institution: | Department of Chemistry, University of Ruhuna, Matara, Sri Lanka, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 5a Pawińskiego, 02-106 Warsaw, Poland. |
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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. |
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