Jaravine Victor A, Cordier Florence, Grzesiek Stephan
Division of Structural Biology, Biozentrum der Universität Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
J Biomol NMR. 2004 Jul;29(3):309-18. doi: 10.1023/B:JNMR.0000032516.87434.35.
The effect of hydrogen/deuterium exchange on protein hydrogen bond coupling constants (h3)J(NC') has been investigated in the small globular protein ubiquitin. The couplings across deuterated or protonated hydrogen bonds were measured by a long-range quantitative HA(CACO)NCO experiment. The analysis is combined with a determination of the H(N)/D(N) isotope effect on the amide group (1)J(NC') couplings and the (15)N and (13)C' chemical shifts. On average, H-bond deuteration exchange weakens (h3)J(NC') and strengthens (1)J(NC') couplings. A correlation is found between the size of the (15)N isotope shift, the (15)N chemical shift, and the (h3)J(NC') coupling constants. The data are consistent with a reduction of donor-acceptor overlap as expected from the classical Ubbelohde effect and the common understanding that H(N)/D(N) exchange leads to a shortening of the N-hydron bond length.
已在小分子球状蛋白泛素中研究了氢/氘交换对蛋白质氢键耦合常数（h3）J(NC')的影响。通过远程定量HA(CACO)NCO实验测量了跨越氘化或质子化氢键的耦合。该分析结合了对酰胺基团（1）J(NC')耦合以及（15）N和（13）C'化学位移的H(N)/D(N)同位素效应的测定。平均而言，氢键氘化交换会削弱（h3）J(NC')并增强（1）J(NC')耦合。发现（15）N同位素位移大小、（15）N化学位移与（h3）J(NC')耦合常数之间存在相关性。这些数据与经典乌布勒德效应预期的供体-受体重叠减少以及H(N)/D(N)交换导致N-氢原子键长度缩短的普遍认识一致。
