NOVEL STRATEGIES FOR BACKBONE & SIDECHAIN ASSIGNMENT IN SOLID PHASE POLYPEPTIDES

异核和同核主链和侧链的相关性是 对多标记多肽的核磁共振指认必不可少 处于固定化状态的蛋白质。关联通常被检索到 从多维(‘H，13C’i‘N)相关实验中，我们 证明，或者，少量一维的 利用选择性和高效异核进行的实验 极化转移可用于主干分配。我们也 演示如何将此方法扩展到侧链分配 同核通键，通过空间或质子介导的转移 技巧。特别地，我们研究了偏振传递 三肽(NH，Cal CP)亚系统的动力学研究 多自旋系统的理论预测的结果。这些 实验协议可以在任意MAS频率下使用 并且对于所施加的r.f的大小是非常宽容的。 菲尔兹。

Hetero- and homonuclear backbone and sidechain correlations are essential for NMR assignments in multiply labeled peptides and proteins in the immobilized state. Correlations are usually retrieved from multi-dimensional ('H, 13C'I 'N) correlation experiments. We demonstrate that, alternatively, a small number of one-dimensional experiments employing selective and efficient heteronuclear polarization transfer can be used for backbone assignments. We also show how this approach can be extended for sidechain assignments using homonuclear through-bond, through space or proton-mediated transfer techniques. In particular, we investigate the polarization transfer dynamics in (NH, Cal Cp) subsystems of a tripeptide and compare our results to theoretical predictions in multi-spin systems. These experimental protocols can be employed at arbitrary MAS frequencies and are very forgiving with respect to the size of the applied r. f. fields.