Bernadó Pau, Blackledge Martin
Institut de Biologie Structurale - Jean-Pierre Ebel C.N.R.S.-C.E.A.-UJF 41, rue Jules Horowitz - 38027 Grenoble Cedex - France.
J Am Chem Soc. 2004 Jun 30;126(25):7760-1. doi: 10.1021/ja048785m.
Local protein backbone dynamics on time scales reaching up to milliseconds have been investigated using residual dipolar couplings (RDC) using an analytical description of conformational averaging under the influence of anisotropic peptide plane dynamics. We have applied this technique to RDC from protein G and find that sites in the alpha-helix exhibit overall higher-order parameters than loops, suggesting a high degree of conformational integrity even over this extended time period. The approach is shown to be stable when using data from a smaller number of alignment media. Order parameters derived from combinations of independent subsets of two and three of the five alignment media from protein G reveal results essentially identical to those from the complete data set. Structures of lysozyme determined at different crystal diffraction resolutions ranging from 0.9 to 2.1 A give similar dynamic parameters using this method, demonstrating robustness with respect to structural error.
利用残余偶极耦合（RDC），通过对各向异性肽平面动力学影响下的构象平均进行解析描述，研究了时间尺度长达毫秒级的局部蛋白质主链动力学。我们已将此技术应用于来自蛋白G的RDC，发现α螺旋中的位点比环区表现出更高的序参数，这表明即使在这段较长的时间内，也具有高度的构象完整性。当使用来自较少数量排列介质的数据时，该方法显示出稳定性。从蛋白G的五种排列介质中的两种和三种的独立子集组合得出的序参数，其结果与来自完整数据集的结果基本相同。使用此方法，在0.9至2.1埃不同晶体衍射分辨率下测定的溶菌酶结构给出了相似的动力学参数，证明了该方法对于结构误差的稳健性。
