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

• Autorzy: Lankiewicz L. , Malicka J. , Wiczk W.
• Języki publikacji: EN

Abstrakty

EN

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 K2 value on FRET results and determinants of k2 are discussed.

Słowa kluczowe

EN

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

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1997
• Tom: 44
• Numer: 3
• Opis fizyczny: p.477-489

Twórcy

autor

Lankiewicz L.

• University of Gdansk, J.Sobieskiego 18, 80-952 Gdansk, Poland

autor

Malicka J.

autor

Wiczk W.

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