Gitti Rossitza K, Wright Nathan T, Margolis Joyce W, Varney Kristen M, Weber David J, Margolis Frank L
Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 North Greene Street, Baltimore, Maryland 21201, USA.
Biochemistry. 2005 Jul 19;44(28):9673-9. doi: 10.1021/bi050149t.
Nuclear magnetic resonance (NMR) (15)N relaxation measurements of the olfactory marker protein (OMP) including longitudinal relaxation (T(1)), transverse relaxation (T(2)), and (15)N-{(1)H} NOE data were collected at low protein concentrations (<or=100 microM) 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)/D( perpendicular) = 1.20 +/- 0.02 with an overall global correlation time of 8.93 +/- 0.03 ns. 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 (alpha1), 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.
在低蛋白浓度（≤100微摩尔）以及两种场强（14.4和18.8特斯拉）条件下，对162个主链酰胺基团中的135个进行了嗅觉标记蛋白（OMP）的核磁共振（NMR）（15）N弛豫测量，包括纵向弛豫（T(1)）、横向弛豫（T(2)）以及（15）N-{(1)H}核Overhauser效应（NOE）数据收集。发现OMP的旋转扩散呈轴对称，D(平行)/D(垂直)=1.20±0.02，整体全局相关时间为8.93±0.03纳秒。对这些数据进行的无模型内部动力学分析描述了该蛋白在多个时间尺度上的动力学。这些研究结果表明，α-螺旋1（α1）、环1和保守的Ω环（环3）具有很大程度的构象灵活性。讨论了OMP这些动态区域在调节嗅觉信号转导中的功能意义。
