MAPPING GLOBAL FOLDS OF OLIGONUCLEOTIDES BY PULSED ELECTRON-ELECTRON DOUBLE RESONANCE

被引:20
|
作者
Schiemann, Olav [1 ]
机构
[1] Univ St Andrews, Ctr Magnet Resonance, Ctr Biomol Sci, St Andrews, Fife, Scotland
来源
METHODS IN ENZYMOLOGY, VOL 469: BIOPHYSICAL, CHEMICAL, AND FUNCTIONAL PROBES OF RNA STRUCTURE, INTERACTIONS AND FOLDING, PT B | 2009年 / 469卷
关键词
PARAMAGNETIC-RESONANCE; HAMMERHEAD RIBOZYME; SPIN-ECHO; METAL-ION; DISTANCE MEASUREMENTS; PELDOR MEASUREMENTS; EPR SPECTROSCOPY; BINDING-SITES; ELDOR; MODEL;
D O I
10.1016/S0076-6879(09)69016-9
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The understanding of structure-dynamics-function relationships in oligonucleotides or oligonucleotide/protein complexes calls for biophysical methods that can resolve the structure and dynamics of such systems on the critical nanometer length scale. A modern electron paramagnetic resonance (EPR) method called pulsed electron-electron double resonance (PELDOR or DEER) has been shown to reliably and precisely provide distances and distance distributions in the range of 1.5-8 nm. In addition, recent experiments proved that a PELDOR experiment also contains information on the orientation of labels, enables easy separation of coupling mechanisms and allows for counting the number of monomers in complexes. This chapter briefly summarizes the theory, describes how to perform and analyze such experiments and discusses the limitations.
引用
收藏
页码:329 / 351
页数:23
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