RESIDUAL DIPOLAR COUPLINGS FOR REFINEMENT OF PROTEIN STRUCTURES

用于细化蛋白质结构的残余偶极偶联

• 批准号: 6298151
• 负责人: STEPHEN FESIK
• 金额: $ 0.75万
• 依托单位: UNIVERSITY OF WISCONSIN-MADISON
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-03-01 至 2000-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6298151
• 关键词: biomedical resource; nuclear magnetic resonance spectroscopy; structural biology; technology /technique

Recently, NMR methods have been developed to accurately measure one bond 1JNH coupling constants. The apparent 1JNH coupling constant is the sum of the scalar coupling and the residual dipolar coupling. Since the residual dipolar coupling is proportional to the square of the static field and the scalar coupling is constant as a function of field strength, residual dipolar couplings can be measured from the field dependnece of the apparent 1JNH coupling constants. Residual dipolar couplings occur due to the partial ordering of a molecule in the magnetic field and are related to the angle between the N-H bond vector and the magnetic susceptibility tensor. Thus, it has been suggested that residual dipolar couplings could be used as additional constraints in the structure determination of proteins. We propose to measure the residual dipolar couplings for several proteins to determine whether this is a useful constraint in the structure determination of proteins. Although we have access to a 500 and 600 MHz NMR spectrometer for measuring one bond couplings, we need to measure these couplings at higher fields to reliably derive the residual dipolar couplings from the field dependence of the observed 1JNH coupling constants.

最近，核磁共振方法已被开发出来，可以精确测量 一键 1JNH 耦合常数。 表观 1JNH 耦合常数 是标量耦合和残余偶极耦合之和。 由于残余偶极耦合与 静态场和标量耦合是恒定的函数 场强，残余偶极耦合可以从测量 表观 1JNH 耦合常数的场依赖性。 残差 偶极耦合是由于分子的偏序而发生的 磁场 和 N-H 键之间的角度有关 矢量和磁化率张量。 于是，就已经 建议剩余偶极耦合可以用作附加 蛋白质结构测定的限制。 我们建议 测量几种蛋白质的残余偶极耦合 确定这是否是结构中有用的约束 蛋白质的测定。 虽然我们可以使用 500 和 600 MHz NMR 波谱仪用于测量单键耦合，我们需要 在更高的场测量这些耦合，以可靠地得出 观测到的场依赖性的残余偶极耦合 1JNH耦合常数。