Moon Seongho, Case David A
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
J Biomol NMR. 2007 Jun;38(2):139-50. doi: 10.1007/s10858-007-9156-8. Epub 2007 Apr 14.
We propose a new computational model to predict amide proton chemical shifts in proteins. In addition to the ring-current, susceptibility and electrostatic effects of earlier models, we add a hydrogen-bonding term based on density functional calculations of model peptide-peptide and peptide-water systems. Both distance and angular terms are included, and the results are rationalized in terms of natural bond orbital analysis of the interactions. Comparison to observed shifts for 15 proteins shows a significant improvement over existing structure-shift correlations. These additions are incorporated in a new version of the SHIFTS program.
我们提出了一种新的计算模型来预测蛋白质中酰胺质子的化学位移。除了早期模型中的环电流、磁化率和静电效应外，我们还基于模型肽-肽和肽-水体系的密度泛函计算添加了一个氢键项。同时包含了距离项和角度项，并根据相互作用的自然键轨道分析对结果进行了合理解释。与15种蛋白质的观测位移进行比较，结果表明与现有的结构-位移相关性相比有显著改进。这些新增内容已被纳入SHIFTS程序的新版本中。
