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• W2022778461 endingPage "4178" @default.
• W2022778461 startingPage "4168" @default.
• W2022778461 abstract "Molecular dynamics simulations were used to examine the structural dynamics of two fluorescent probes attached to a typical protein, hen egg-white lysozyme (HEWL). The donor probe (D) was attached via a succinimide group, consistent with the commonly-used maleimide conjugation chemistry, and the acceptor probe (A) was bound into the protein as occurs naturally for HEWL and the dye Eosin Y. The <kappa(2)> is found to deviate significantly from the theoretical value and high correlation between the orientation factor kappa and the distance R is observed. The correlation is quantified using several possible fixed A orientations and correlation as high as 0.80 is found between kappa and R and as high as 0.68 between kappa(2) and R. The presence of this correlation highlights the fact that essentially all fluorescence-detected resonance energy transfer studies have assumed that kappa and R are independent--an assumption that is clearly not justified in the system studied here. The correlation results in the quantities <kappa(2)R(-)(6)> and <kappa(2)> < R(-)(6)> differing by a factor of 1.6. The observed correlation between kappa and R is caused by the succinimide linkage between the D and HEWL, which is found to be relatively inflexible." @default.
• W2022778461 created "2016-06-24" @default.
• W2022778461 creator A5012410432 @default.
• W2022778461 creator A5043265945 @default.
• W2022778461 creator A5049000902 @default.
• W2022778461 creator A5085210707 @default.
• W2022778461 date "2007-06-01" @default.
• W2022778461 modified "2023-09-30" @default.
• W2022778461 title "Fretting about FRET: Correlation between κ and R" @default.
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• W2022778461 doi "https://doi.org/10.1529/biophysj.106.092650" @default.
• W2022778461 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1877789" @default.
• W2022778461 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17384068" @default.
• W2022778461 hasPublicationYear "2007" @default.
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