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 |
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頁(從 - 到) | 1037-1040 |
頁數 | 4 |
期刊 | Magnetic Resonance in Chemistry |
卷 | 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