Paramagnetic tagging for protein structure and dynamics analysis

被引:130
作者
Keizers, Peter M. [1 ]
Ubbink, Marcellus [1 ]
机构
[1] Leiden Univ, Leiden Inst Chem, Gorlaeus Labs, NL-2300 RA Leiden, Netherlands
关键词
Protein NMR spectroscopy; Paramagnetic probes; Lanthanide tags; Pseudocontact shifts; Magnetic field alignment; Paramagnetic relaxation enhancement; NUCLEAR-MAGNETIC-RESONANCE; RESIDUAL DIPOLAR COUPLINGS; LANTHANIDE-BINDING TAG; SITE-DIRECTED SPIN; TRANSIENT ENCOUNTER COMPLEXES; ELECTRON-TRANSFER COMPLEX; CYTOCHROME-C PEROXIDASE; NMR-SPECTROSCOPY; RELAXATION ENHANCEMENT; SHIFT-REAGENT;
D O I
10.1016/j.pnmrs.2010.08.001
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Researchers have developed paramagnetic tagging for protein structure and dynamics analysis by using Nuclear Magnetic Resonance (NMR) spectra. They have demonstrated that paramagnetic centers are characterized by two properties that determine the type of restraints they generate. It has been observed that centers with slow electronic relaxation cause strong Paramagnetic Relaxation Enhancement (PRE), while the effect of centers with fast electronic relaxation on nuclear relaxation is much smaller. The anisotropy of the paramagnetic effect, described by the magnetic susceptibility tensor, causes line shifts, along with partial alignment of molecules in strong magnetic fields. A variety of paramagnetic tags has been developed and improved, each with its own properties. The simplest and most widely used paramagnetic tags are the nitroxide spin labels.
引用
收藏
页码:88 / 96
页数:9
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