Siemer Ansgar B, Arnold Alexandre A, Ritter Christiane, Westfeld Thomas, Ernst Matthias, Riek Roland, Meier Beat H
Physical Chemistry, ETH Zurich, CH-8093 Zurich, Switzerland.
J Am Chem Soc. 2006 Oct 11;128(40):13224-8. doi: 10.1021/ja063639x.
We report the observation of undetected (until now) residues of the prion protein fragment HET-s(218-289) which give rise to well-resolved (13)C, (15)N, and (1)H NMR resonances under high-resolution magic-angle spinning (HRMAS) conditions. The observed signals belong to large polymeric units as shown by measuring the lateral diffusion constants. The amino acids identified in the spectra are compatible with their localization in the segments of the protein which could not be detected in earlier solid-state NMR experiments. The observed chemical shifts indicate that these residues are in a random-coil conformation. Complementary experiments which detect only dynamic or static residues, respectively, strongly suggest that they belong to different parts of the same molecule.
我们报告了对朊病毒蛋白片段HET-s(218 - 289)未检测到的（直至目前）残留物的观察结果，这些残留物在高分辨率魔角旋转(HRMAS)条件下产生了分辨率良好的(13)C、(15)N和(1)H NMR共振。如通过测量横向扩散常数所示，观察到的信号属于大型聚合物单元。光谱中鉴定出的氨基酸与它们在蛋白质片段中的定位相符，这些片段在早期的固态NMR实验中无法检测到。观察到的化学位移表明这些残基处于无规卷曲构象。分别仅检测动态或静态残基的补充实验强烈表明它们属于同一分子的不同部分。
