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Backbone dynamics of the olfactory marker protein as studied by N-15 NMR relaxation measurements

机译:通过N-15 NMR弛豫测量研究的嗅觉标记蛋白的骨干动力学

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摘要

Nuclear magnetic resonance (NMR) N-15 relaxation measurements of the olfactory marker protein (OMP) including longitudinal relaxation (T-1), transverse relaxation (T-2), and N-15-{H-1} NOE data were collected at low protein concentrations (<= 100 mu M) and at two field strengths (14.4 and 18.8 T) for 135 of 162 backbone amide groups. Rotational diffusion of the OMP was found to be axially symmetric with D-parallel to/D-perpendicular to = 1.20 +/- 0.02 with an overall global correlation time of 8.93 +/- 0.03 us. Model-free internal dynamic analyses of these data provided a description of the protein's dynamics on multiple time scales. The results of these studies indicate that there is a large degree of conformational flexibility for alpha-helix 1 (alpha 1), loop 1, and the conserved Omega-loop (loop 3). The functional significance that these dynamic regions of OMP have in modulating olfactory signal transduction is discussed.
机译:收集嗅觉标记蛋白(OMP)的N-15弛豫测量值,包括纵向弛豫(T-1),横向弛豫(T-2)和N-15- {H-1} NOE数据在162个骨架酰胺基团中的135个处于低蛋白质浓度(<= 100μM)和两个电场强度(14.4和18.8 T)的条件下。发现OMP的旋转扩散是轴对称的,D平行于/ D垂直于= 1.20 +/- 0.02,总的全局相关时间为8.93 +/- 0.03us。这些数据的无模型内部动力学分析提供了在多个时间尺度上蛋白质动态的描述。这些研究的结果表明,α-螺旋1(α1),环1和保守的Omega环(环3)具有很大的构象灵活性。讨论了OMP的这些动态区域在调节嗅觉信号转导中的功能意义。

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