Fluorescence resonance energy transfer in studies of inter-chromophoric distances in biomolecules

被引：42

作者：

Lankiewicz, L ^{[1
]}

Malicka, J ^{[1
]}

Wiczk, W ^{[1
]}

机构：

[1] UNIV GDANSK,FAC CHEM,PL-80952 GDANSK,POLAND

来源：

ACTA BIOCHIMICA POLONICA | 1997年 / 44卷 / 03期

关键词：

fluorescence resonance energy transfer; interchromophoric distance; biomolecule; proteins; conformation;

D O I：

10.18388/abp.1997_4398

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Fluorescence resonance energy transfer (FRET) is a technique widely used in studies of interchromophoric distances in biomolecules such as peptides, proteins and nucleic acids. FRET is especially useful in determination of conformational changes caused by a solvent, presence of denaturing agents, diffusion and other external factors. Precision of interchromophoric distances obtained using the FRET technique is comparable with that of low-resolution X-ray diffraction and NMR data. Comparison of FRET results with the crystal structure for several proteins is reviewed. Moreover, the effect of the orientation factor kappa(2) value on FRET results and determinants of kappa(2) are discussed.

引用

页码：477 / 489

页数：13

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