Measuring distances within unfolded biopolymers using fluorescence resonance energy transfer: The effect of polymer chain dynamics on the observed fluorescence resonance energy transfer efficiency
AUTOR(ES)
Makarov, Dmitrii E.
FONTE
American Institute of Physics
RESUMO
Recent years have seen a number of investigations in which distances within unfolded proteins, polypeptides, and other biopolymers are probed via fluorescence resonance energy transfer, a method that relies on the strong distance dependence of energy transfer between a pair of dyes attached to the molecule of interest. In order to interpret the results of such experiments it is commonly assumed that intramolecular diffusion is negligible during the excited state lifetime. Here we explore the conditions under which this “frozen chain” approximation fails, leading to significantly underestimated donor-acceptor distances, and describe a means of correcting for polymer dynamics in order to estimate these distances more accurately.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2754924Documentos Relacionados
- The estimation of distances between specific backbone-labeled sites in DNA using fluorescence resonance energy transfer.
- Fluorescence Resonance Energy Transfer Microscopy of the Helicobacter pylori Vacuolating Cytotoxin within Mammalian Cells
- Kinking of DNA and RNA helices by bulged nucleotides observed by fluorescence resonance energy transfer.
- Studies on the structure and dynamics of the human telomeric G quadruplex by single-molecule fluorescence resonance energy transfer
- Conformational changes between the active-site and regulatory light chain of myosin as determined by luminescence resonance energy transfer: The effect of nucleotides and actin