Membrane Binding of MARCKS-Related Protein Studied by Tryptophan Fluorescence Spectroscopy

2000 ◽  
Vol 380 (2) ◽  
pp. 380-386 ◽  
Author(s):  
Arndt A.P. Schmitz ◽  
Andreas Ulrich ◽  
Guy Vergères
Keyword(s):  
Fluorescence Spectroscopy ◽  
Membrane Binding ◽  
Tryptophan Fluorescence ◽  
Related Protein

scholarly journals Interaction of caldesmon with phospholipids

1993 ◽  
Vol 291 (2) ◽  
pp. 403-408 ◽  
Author(s):  
E A Czuryło ◽  
J Zborowski ◽  
R Dabrowska
Keyword(s):  
Fluorescence Spectroscopy ◽  
Hydrophobic Interactions ◽  
Tryptophan Fluorescence ◽  
Terminal Part ◽  
Strong Binding ◽  
Terminal Fragment ◽  
Electrostatic And Hydrophobic Interactions ◽  
The Stability

The interaction of caldesmon with liposomes composed of various phospholipids has been examined by tryptophan fluorescence spectroscopy. The results indicate that caldesmon makes its strongest complex with phosphatidylserine (PS) vesicles (Kass. = 1.45 x 10(5) M-1). Both electrostatic and hydrophobic interactions contribute to the stability of this complex. The site for strong binding of PS seems to be located in the N-terminal part of the 34 kDa C-terminal fragment of caldesmon. Binding of PS at this site results in displacement of calmodulin from its complex with caldesmon.

scholarly journals Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Paulina Sindrewicz ◽  
Xiaoxin Li ◽  
Edwin A. Yates ◽  
Jeremy E. Turnbull ◽  
Lu-Yun Lian ◽  
...  
Keyword(s):  
Fluorescence Spectroscopy ◽  
Tryptophan Fluorescence ◽  
Intrinsic Tryptophan Fluorescence ◽  
Ligand Interactions

scholarly journals Ligand-induced conformation change in folate-binding protein

1993 ◽  
Vol 292 (3) ◽  
pp. 921-925 ◽  
Author(s):  
N C Kaarsholm ◽  
A M Kolstrup ◽  
S E Danielsen ◽  
J Holm ◽  
S I Hansen
Keyword(s):  
Fluorescence Spectroscopy ◽  
Ligand Binding ◽  
Binding Protein ◽  
Simultaneous Detection ◽  
Tryptophan Fluorescence ◽  
Random Coil ◽  
Folate Binding Protein ◽  
Beta Strand ◽  
Process Detection ◽  
Induced Aggregation

C.d. and fluorescence spectroscopy have been used to investigate the effect of ligand binding on the structure and stability of folate-binding protein (FBP) from cow's whey. The c.d. spectrum of unligated FBP predicts the following secondary structure: 22% helix, 25% antiparallel beta-strand, 5% parallel beta-strand, 17% turn and 31% random-coil structure. Folate binding to FBP results in significant changes in the c.d. spectrum. Analysis of the spectrum shows a 10% decrease in antiparallel beta-strand as a result of ligand binding. Folate binding also leads to strong quenching of FBP tryptophan fluorescence. The magnitude of the quench is proportional to ligand binding. The guanidinium chloride-induced unfolding of FBP is shown to be a multistate process. Detection by c.d. and fluorescence spectroscopy lead to non-identical transitions. Modelling studies are consistent with the existence of a stable folding intermediate. Ligand binding to FBP increases the apparent folding stability of the molecule. Simultaneous detection by c.d. and fluorescence indicate that the apparent increased folding stability is derived from ligand-induced aggregation of FBP.

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