Direct NMR resonance assignments of the active site histidine residue in Escherichia coli thioesterase I/protease I/lysophospholipase L1

Wen Jin Wu*, Sergiy I. Tyukhtenko, Tai Huang Huang

*此作品的通信作者

研究成果: 雜誌貢獻期刊論文同行評審

1 引文 斯高帕斯(Scopus)

摘要

Owing to the hydrogen-bond interaction and rapid exchange rate with the bulk water, the transverse relaxation time for the Nδ1-H proton of the catalytic histidine in Escherichia coli thioesterase I/protease I/lysophospholipase L1 (TEP-I) is rather short. Because of its catalytic importance, it is desirable to detect and assign this proton resonance. In this paper, we report the first direct NMR correlation between the short-lived Nδ1-H proton and its covalently attached N δ1-nitrogen of the catalytic His157 residue in E. coli thioesterase/protease I. We have used gradient-enhanced jump-return spin-echo HMQC (GE-JR SE HMQC) to obtain a direct correlation between the short-lived Nδ1-H proton and its covalently attached Nδ1- nitrogen. The sensitivity of detection for the short-lived Nδ1- H proton was enhanced substantially by improved water suppression, in particular, the suppression of radiation damping via pulsed field gradients.

原文英語
頁(從 - 到)1037-1040
頁數4
期刊Magnetic Resonance in Chemistry
44
發行號11
DOIs
出版狀態已發佈 - 2006 11月

ASJC Scopus subject areas

  • 一般化學
  • 一般材料科學

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