首页 | 本学科首页   官方微博 | 高级检索  
     检索      

~1H SPIN SYSTEM IDENTIFICATIONS OF S-SULFONATED INSULIN B CHAIN WITH 2D-NMR
作者姓名:华庆新
作者单位:Institute of
基金项目:a grant (DK-34035) from the National Institutes of Health, U.S.A. and a grant (Biol-85-114) from the National Natural Science Foundation of China. The 500 MHz NMR measurements were taken in the National Institute for Medical Researc
摘    要:Resonance assignments of the ~1H spectrum of insulin are the basis on which to investi-gate its solution conformation by using NMR method. Owing to the complicated aggregationbehaviour of the molecule to give broadened n. m. r. lines, only limited resonance assignmentshave been reported. S-sulfonated A and B chains of insulin gave ~1H spectra with good reso-lutions. Based on the 500 MHz absolute 2D-COSY spectrum and 400 MHz phase sensitiveDQF-COSY, Relayed-COSY and NOESY spectra of B chain recorded in D_2O, all of thespin system identifications of the non-labile protons in the S-sulfonated B chain of insulinwere reported including the specific resonance assignments of eight residues: B_3Asn, B_9Ser,B_(16)Tyr, B_(22)Arg, B_(26)Tyr, B_(27)Thr, B_(28)Pro and B_(29)Lys. The pK values of B_(16) and B_(26) tyrosineare 10.65 and 10.60 respectively from pH titration.


~1H SPIN SYSTEM IDENTIFICATIONS OF S-SULFONATED INSULIN B CHAIN WITH 2D-NMR
HUA QING-XIN Institute of Biophysics,Academia Sinica,Beijing.~1H SPIN SYSTEM IDENTIFICATIONS OF S-SULFONATED INSULIN B CHAIN WITH 2D-NMR[J].Science in China(Chemistry),1989(8).
Authors:HUA QING-XIN Institute of Biophysics  Academia Sinica  Beijing
Abstract:Resonance assignments of the ~1H spectrum of insulin are the basis on which to investi-gate its solution conformation by using NMR method. Owing to the complicated aggregationbehaviour of the molecule to give broadened n. m. r. lines, only limited resonance assignmentshave been reported. S-sulfonated A and B chains of insulin gave ~1H spectra with good reso-lutions. Based on the 500 MHz absolute 2D-COSY spectrum and 400 MHz phase sensitiveDQF-COSY, Relayed-COSY and NOESY spectra of B chain recorded in D_2O, all of thespin system identifications of the non-labile protons in the S-sulfonated B chain of insulinwere reported including the specific resonance assignments of eight residues: B_3Asn, B_9Ser,B_(16)Tyr, B_(22)Arg, B_(26)Tyr, B_(27)Thr, B_(28)Pro and B_(29)Lys. The pK values of B_(16) and B_(26) tyrosineare 10.65 and 10.60 respectively from pH titration.
Keywords:insulin  S-sulfonated B chain  2D-NMR
本文献已被 CNKI 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号