AN EFFICIENT 3D NMR TECHNIQUE FOR CORRELATING THE PROTON AND NITROGEN-15 BACKBONE AMIDE RESONANCES WITH THE ALPHA-CARBON OF THE PRECEDING RESIDUE IN UNIFORMLY NITROGEN-15 TO CARBON-13 ENRICHED PROTEINS

AN EFFICIENT 3D NMR TECHNIQUE FOR CORRELATING THE PROTON AND NITROGEN-15 BACKBONE AMIDE RESONANCES WITH THE ALPHA-CARBON OF THE PRECEDING RESIDUE IN UNIFORMLY NITROGEN-15 TO CARBON-13 ENRICHED PROTEINS
复制标题

DOI:
10.1007/bf01874573
复制
发表时间:
1991-01-01
影响因子:
2.7
通讯作者:
IKURA M
IKURA M
中科院分区:
生物学3区
文献类型:
--
作者:
BAX A;IKURA M

文献摘要

被引文献

相似文献

描述了一种3D NMR技术,其将氨基酸残基的酰胺质子和氮共振与C α相关联。其前一个残基的化学位移。该技术使用中继机制,将磁化强度从15 N转移到13 C α。通过插入的羰基核。这种获得连续连接性的方法对大线宽的敏感性低于另一种HNCA实验。该技术被证明为蛋白质钙调素,与骨骼肌肌球蛋白轻链激酶的26个氨基酸片段复合。
A 3D NMR technique is described which correlates the amide proton and nitrogen resonances of an amino acid residue wth the C.alpha. chemical shift of its preceding residue. The technique uses a relay mechanism, transferring magnetization from 15N to 13C.alpha. via the intervening carbonyl nucleus. This method for obtaining sequential connectivity is less sensitive to large line widths than the alternative HNCA experiment. The technique is demonstrated for the protein calmodulin, complexed with a 26 amino acid fragment of skeletal muscle myosin light chain kinase.