Comparison of Solid-State Dipolar Couplings and Solution Relaxation Data Provides Insight into Protein Backbone Dynamics

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• 作者：Veniamin Chevelkov ; Yi Xue ; Rasmus Linser ; Nikolai R. Skrynnikov ; Bernd Reif
• 刊名：Journal of the American Chemical Society
• 出版年：2010
• 出版时间：April 14, 2010
• 年：2010
• 卷：132
• 期：14
• 页码：5015-5017
• 全文大小：157K
• 年卷期：v.132,no.14(April 14, 2010)
• ISSN：1520-5126

文摘

Analyses of solution ¹⁵N relaxation data and solid-state ¹H^N−¹⁵N dipolar couplings from a small globular protein, α-spectrin SH3 domain, produce a surprisingly similar pattern of order parameters. This result suggests that there is little or no ns−μs dynamics throughout most of the sequence and, in particular, in the structured portion of the backbone. At the same time, evidence of ns−μs motions is found in the flexible loops and termini. These findings, corroborated by the MD simulations of α-spectrin SH3 in a hydrated crystalline environment and in solution, are consistent with the picture of protein dynamics that has recently emerged from the solution studies employing residual dipolar couplings.