Decay of Fluorescence

Stern, O.; Volmer, Max

doi:10.1259/jrs.1919.0087

Cited by 208 publications

(240 citation statements)

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“…For this reason, a control experiment was carried out in which the shortening of monomer's life time rather than Fe/F m ratio was measured to determine the excimermonomer ratio. The pyrene excimerization is a process of the dynamic quenching of monomer fluorescence [ 16] and hence should be described by Stern-Volmer equation [20]:…”

Section: Resultsmentioning

confidence: 99%

The increase of phospholipid bilayer rigidity after lipid peroxidation

Dobretsov¹,

Borschevskaya²,

Петров³

et al. 1977

FEBS Letters

277

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Section: Resultsmentioning

confidence: 99%

The increase of phospholipid bilayer rigidity after lipid peroxidation

Dobretsov¹,

Borschevskaya²,

Петров³

et al. 1977

FEBS Letters

277

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“…The KI solution used contained 0.1 mM sodium thiosulfate to inhibit formation of 13- (Wasylewski et al, 1988). The quenching constant KQ was determined according to the Stern-Volmer theory (Stern & Volmer, 1919).…”

Section: Methodsmentioning

confidence: 99%

Shape and lipid-binding site of the nonspecific lipid-transfer protein (sterol carrier protein 2): A steady-state and time-resolved fluorescence study

Gadella¹,

Bastiaens²,

Visser³

et al. 1991

Biochemistry

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“…All measurements were carried out at 25°C with excitation and emission lights of 390 and 500 nm, respectively. Data were shown as Stern-Volmer plots to obtain the quenching constant, K SV (36).…”

Section: Methodsmentioning

confidence: 99%

ATP-induced Opposite Changes in the Local Environments around Cys697 (SH2) and Cys707 (SH1) of the Myosin Motor Domain Revealed by the Prodan Fluorescence

Hiratsuka

1999

Journal of Biological Chemistry

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To obtain a consistent view of the nucleotide-induced conformational changes around Cys 697 (SH2) and Cys 707(SH1) in skeletal myosin subfragment-1 (S-1), the two thiols were labeled with the same environmentally sensitive fluorophore, 6-acyl-2-dimethylaminonaphthalene group, using 6-acryloyl-2-dimethylaminonaphthalene (acrylodan, AD) and 6-bromoacetyl-2-dimethylaminonaphthalene (BD), respectively. The resultant fluorescent derivatives, AD-S-1 and BD-S-1, have the same fluorophore at either SH2 or SH1, which was verified by inspections of changes in the ATPases and the localization of fluorescence after tryptic digestion and CNBr cleavage for the two derivatives. Especially, AD was found to be a very useful fluorescent reagent that readily reacts with only SH2 of S-1. Measurements of the nucleotideinduced changes in fluorescence emission spectra of AD-S-1 and BD-S-1 suggested that during ATP hydrolysis the environment around the fluorophore at SH2 is very distinct from that around the fluorophore at SH1, being defined as that the former has the hydrophobic and closed characteristics, whereas the latter has the hydrophilic and open ones. The KI quenching study of the fluorescence of the two S-1 derivatives confirmed these results. The most straightforward interpretation for the present results is that during ATP hydrolysis, the helix containing SH2 is buried in hydrophobic side chains and rather reinforced, whereas the adjacent helix containing SH1 moves away from its stabilizing tertiary structural environment.The structural element of the molecular motor myosin is the subfragment-1 (S-1) 1 moiety that contains the sites responsible for the ATP hydrolysis and binding of actin (1). A striking feature of the S-1 structure is a long helix spanning 85 Å that is stabilized by interactions with the myosin light chains (2). It has been proposed that this light chain-binding domain acts as a semi rigid "lever arm" to amplify and transmit conformational changes in the ATP and actin binding sites of S-1 (3-9).Cys 707 (SH1) and Cys 697 (SH2) are located on the two different helixes in the C-terminal segment of the S-1 catalytic domain and separated from one another by 19 Å (2). The two helixes are kinked at a conserved glycine residue (Gly 699 ) found in a bend joining two helixes. Recent experiments have led to a conclusion that the fulcrum point for the swinging motion of the lever arm is in the vicinity of the SH1-SH2 region (4 -9). Furthermore, Gly 699 (close to SH2) and Gly 710 (close to SH1) have been proposed to act as pivot points or flexible hinges for such motion (8,10,11). These data show the importance of motion in the SH1-SH2 region in the force generation cycle of myosin. However, the precise conformational changes of this region that are involved in lever arm movement are still unknown.One approach for understanding the involvement of the SH1-SH2 region in lever arm movement is a precise comparison of the individual conformational changes around SH1 and SH2 during ATPase cycle of S-1. Such a study could...

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Decay of Fluorescence

Cited by 208 publications

References 0 publications

The increase of phospholipid bilayer rigidity after lipid peroxidation

The increase of phospholipid bilayer rigidity after lipid peroxidation

Shape and lipid-binding site of the nonspecific lipid-transfer protein (sterol carrier protein 2): A steady-state and time-resolved fluorescence study

ATP-induced Opposite Changes in the Local Environments around Cys697 (SH2) and Cys707 (SH1) of the Myosin Motor Domain Revealed by the Prodan Fluorescence

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