Dependence of the Size of a Protein-SDS Complex on Detergent and Na+ Concentrations

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• 作者：Chinthaka Sanath Gangabadage ; Andzelika Najda ; Diana Bogdan ; Sybren S. Wijmenga ; Marco Tessari
• 刊名：Journal of Physical Chemistry B
• 出版年：2008
• 出版时间：April 10, 2008
• 年：2008
• 卷：112
• 期：14
• 页码：4242 - 4245
• 全文大小：65K
• 年卷期：v.112,no.14(April 10, 2008)
• ISSN：1520-5207

文摘

Sodium dodecyl sulfate (SDS) micelles provide ideal mimetic media for high-resolution NMR studies ofmembrane proteins and proteins or peptides interacting with micellar aggregates. ¹⁵N NMR relaxation of thebackbone 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 NaClconcentrations. A comparison with calculated rotational diffusion times of protein-free SDS micelles underthe same conditions suggests that the size of both aggregates must follow a similar functional dependence ondetergent/NaCl concentration.