Determination of Membrane Protein Structure and Dynamics by Magic-Angle-Spinning Solid-State NMR Spectroscopy

详细信息    查看全文

• 作者：Ovidiu C. Andronesi ; Stefan Becker ; Karsten Seidel ; Henrike Heise ; Howard S. Young ; and Marc Baldus
• 刊名：Journal of the American Chemical Society
• 出版年：2005
• 出版时间：September 21, 2005
• 年：2005
• 卷：127
• 期：37
• 页码：12965 - 12974
• 全文大小：515K
• 年卷期：v.127,no.37(September 21, 2005)
• ISSN：1520-5126

文摘

It is shown that molecular structure and dynamics of a uniformly labeled membrane protein canbe studied under magic-angle-spinning conditions. For this purpose, dipolar recoupling experiments arecombined with novel through-bond correlation schemes that probe mobile protein segments. These NMRschemes are demonstrated on a uniformly [¹³C,¹⁵N] variant of the 52-residue polypeptide phospholamban.When reconstituted in lipid bilayers, the NMR data are consistent with an -helical trans-membrane segmentand a cytoplasmic domain that exhibits a high degree of structural disorder.