Site-specific tryptophan fluorescence spectroscopy as a probe of membrane peptide structure and dynamics

2002 ◽  
Vol 31 (1) ◽  
pp. 9-13 ◽  
Author(s):  
Andrew H. Clayton ◽  
William H. Sawyer
Keyword(s):  
Fluorescence Spectroscopy ◽  
Tryptophan Fluorescence ◽  
Peptide Structure ◽  
Site Specific ◽  
Structure And Dynamics ◽  
Membrane Peptide

Solid-state NMR studies of proteins: the view from static 2H NMR experiments

1998 ◽  
Vol 76 (2-3) ◽  
pp. 411-422 ◽  
Author(s):  
David J Siminovitch
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Integral Membrane Protein ◽  
Peptide Structure ◽  
Nmr Studies ◽  
Dynamic Information ◽  
H Nmr ◽  
Structure And Dynamics ◽  
Oriented Samples ◽  
Membrane Peptide

The application of solid-state 2H NMR spectroscopy to the study of protein and peptide structure and dynamics is reviewed. The advantages of solid-state NMR for the study of proteins are considered, and the particular advantages of solid-state 2H NMR are summarized. Examples of work on the integral membrane protein bacteriorhodopsin, and the membrane peptide gramicidin, are used to highlight the major achievements of the 2H NMR technique. These examples demonstrate that through the use of oriented samples, it is possible to obtain both structural and dynamic information simultaneously.Key words: solid-state NMR, 2H NMR, membrane peptides, membrane proteins, oriented bilayers.

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.

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