Kloiber Karin, Schüler Wolfgang, Konrat Robert
Institute of Organic Chemistry, University of Innsbruck, Austria.
J Biomol NMR. 2002 Apr;22(4):349-63. doi: 10.1023/a:1014936319712.
The simultaneous interpretation of a suite of dipole-dipole and dipole-CSA cross-correlation rates involving the backbone nuclei 13Calpha, 1Halpha, 13CO, 15N and 1HN can be used to resolve the ambiguities associated with each individual cross-correlation rate. The method is based on the transformation of experimental cross-correlation rates via calculated values based on standard peptide plane geometry and solid-state 13CO CSA parameters into a dihedral angle probability surface. Triple resonance NMR experiments with improved sensitivity have been devised for the quantification of relaxation interference between 1Halpha(i)-13Calpha(i)/15N(i)-1HN(i) and 1Halpha(i-1)-13Calpha(i-1)/15N(i)-1HN(i) dipole-dipole mechanisms in 15N, 13C-labeled proteins. The approach is illustrated with an application to 13C, 15N-labeled ubiquitin.
对涉及主链原子核13Cα、1Hα、13CO、15N和1HN的一组偶极-偶极和偶极-CSA交叉相关速率进行同时解释，可用于解决与每个单独交叉相关速率相关的模糊性。该方法基于通过基于标准肽平面几何结构和固态13CO CSA参数的计算值将实验交叉相关速率转换为二面角概率曲面。已设计出具有更高灵敏度的三重共振核磁共振实验，用于定量15N、13C标记蛋白质中1Hα(i)-13Cα(i)/15N(i)-1HN(i)和1Hα(i-1)-13Cα(i-1)/15N(i)-1HN(i)偶极-偶极机制之间的弛豫干扰。通过对13C、15N标记的泛素的应用来说明该方法。
