Sensitivity-enhanced Experiments for the Measurement of J and Dipolar Coupling Constants  

作　　者：林东海 廖新丽 

机构地区：[1]DepartmentofBiochemistry,TheHongKongUniversityofScience＆Technology,HongKong,China

出　　处：《Chinese Journal of Chemistry》2002年第7期623-628,共6页中国化学（英文版）

基　　金：ProjectsupportedbytheNationalNaturalScienceFoundationofChina (No.19975 0 38)

摘　　要：A sensitivity-enhanced IPAP NMR experiment was described in this paper, whichseparates the ~1H-^(15)N doublets into two different spectra to alleviate the problem of resonanceoverlaps and achieve the accurate measurement of J and residual dipolar coupling constants inproteins. This experiment offered 20%―60% sensitivity enhancement over the original IPAPexperiment, and therefore produced more measurable resonances. Pulsed field gradient was used forcoherence selection. Water-flip-back approach was used for water suppression. Thesensitivity-enhanced IPAP experiment was employed in the measurement of ~1J_(NH) and ~1D_(NH)constants of the protein UBC9.A sensitivity-enhanced IPAP NMR experiment was described in this paper, whichseparates the ~1H-^(15)N doublets into two different spectra to alleviate the problem of resonanceoverlaps and achieve the accurate measurement of J and residual dipolar coupling constants inproteins. This experiment offered 20%―60% sensitivity enhancement over the original IPAPexperiment, and therefore produced more measurable resonances. Pulsed field gradient was used forcoherence selection. Water-flip-back approach was used for water suppression. Thesensitivity-enhanced IPAP experiment was employed in the measurement of ~1J_(NH) and ~1D_(NH)constants of the protein UBC9.

关 键 词：J coupling residual dipolar coupling liquid crytalline media spin-stateseparated spectra sensitivity enhancement 

分 类 号：O657.1[理学—分析化学]