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通过灵敏度增强核磁共振光谱法检测中等大小的13C/15N标记蛋白质中非常弱的侧链-主链氢键相互作用。

Detection of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins by sensitivity-enhanced NMR spectroscopy.

作者信息

Liu A, Hu W, Majumdar A, Rosen M K, Patel D J

机构信息

Cellular Biochemistry & Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.

出版信息

J Biomol NMR. 2000 May;17(1):79-82. doi: 10.1023/a:1008373501591.

DOI:10.1023/a:1008373501591
PMID:10909868
Abstract

We describe the direct observation of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins with sensitivity-enhanced NMR spectroscopy. Specifically, the remote correlation. between the hydrogen acceptor side chain carboxylate carbon 13CO2delta of glutamate 54 and the hydrogen donor backbone amide 15N of methionine 49 in a 12 kDa protein, human FKBP12, is detected via the trans-hydrogen bond 3hJ(NCO2delta) coupling by employing a novel sensitivity-enhanced HNCO-type experiment, CPD-HNCO. The 3hJ(NCO2delta) coupling constant appears to be even smaller than the average value of backbone 3hJ(NC') couplings, consistent with more extensive local dynamics in protein side chains.

摘要

我们利用灵敏度增强的核磁共振光谱法，直接观察了中等大小的13C/15N标记蛋白质中非常微弱的侧链-主链氢键相互作用。具体而言，在12 kDa的蛋白质人FKBP12中，通过一种新型的灵敏度增强的HNCO型实验CPD-HNCO，经由反式氢键3hJ(NCO2δ)耦合，检测到了谷氨酸54的氢受体侧链羧基碳13CO2δ与甲硫氨酸49的氢供体主链酰胺15N之间的远程相关性。3hJ(NCO2δ)耦合常数似乎甚至小于主链3hJ(NC')耦合的平均值，这与蛋白质侧链中更广泛的局部动力学一致。

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本文引用的文献

1
Sensitivity enhanced NMR spectroscopy by quenching scalar coupling mediated relaxation: application to the direct observation of hydrogen bonds in 13C/15N-labeled proteins.通过淬灭标量耦合介导的弛豫增强灵敏度的核磁共振光谱法：应用于直接观测13C/15N标记蛋白质中的氢键
J Biomol NMR. 2000 May;17(1):55-61. doi: 10.1023/a:1008340116418.
2
NMR experiments for resonance assignments of 13C, 15N doubly-labeled flexible polypeptides: application to the human prion protein hPrP(23-230).用于13C、15N双标记柔性多肽共振归属的核磁共振实验：应用于人类朊病毒蛋白hPrP(23 - 230)
J Biomol NMR. 2000 Feb;16(2):127-38. doi: 10.1023/a:1008305022907.
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分析 FK506 结合蛋白 FKBP12 的可见构象亚基。
Biochem J. 2013 Aug 1;453(3):371-80. doi: 10.1042/BJ20130276.
4
Direct NMR observation and DFT calculations of a hydrogen bond at the active site of a 44 kDa enzyme.对一种44 kDa酶活性位点处氢键的直接核磁共振观测与密度泛函理论计算
J Biomol NMR. 2002 Sep;24(1):31-9. doi: 10.1023/a:1020697627485.
5
Rapid protein fold determination using secondary chemical shifts and cross-hydrogen bond 15N-13C' scalar couplings (3hbJNC').利用二级化学位移和交叉氢键15N-13C'标量耦合（3hbJNC'）快速确定蛋白质折叠结构
J Biomol NMR. 2001 Nov;21(3):221-33. doi: 10.1023/a:1012935005256.
6
NMR detection of side chain-side chain hydrogen bonding interactions in 13C/15N-labeled proteins.核磁共振检测13C/15N标记蛋白质中侧链-侧链氢键相互作用
J Biomol NMR. 2000 Aug;17(4):305-10. doi: 10.1023/a:1008390813387.
Observation of internucleotide NH...N hydrogen bonds in the absence of directly detectable protons.
在不存在直接可检测质子的情况下对核苷酸间NH...N氢键的观察。
J Biomol NMR. 1999 Nov;15(3):207-11. doi: 10.1023/a:1008357304708.
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Observation of through-hydrogen-bond 2hJHC' in a perdeuterated protein.在全氘代蛋白质中对通过氢键的2hJHC'的观察。
J Magn Reson. 1999 Oct;140(2):510-2. doi: 10.1006/jmre.1999.1899.
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Observation and measurement of internucleotide 2JNN coupling constants between 15N nuclei with widely separated chemical shifts.对具有广泛化学位移的15N核之间的核苷酸间2JNN耦合常数的观察与测量。
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The 2D NMR experiments H(C)CO2 and HCCO2 for assignment and pH titration of carboxylate groups in uniformly 15N/13C-labeled proteins.用于对均匀15N/13C标记蛋白质中羧基进行归属和pH滴定的二维核磁共振实验H(C)CO2和HCCO2 。
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