The spatial orientation of the essential amino acid residues arginine and aspartate within the α1β1 integrin recognition site of collagen IV has been resolved using fluorescence resonance energy transfer

2000 ◽  
Vol 297 (2) ◽  
pp. 501-509 ◽  
Author(s):  
Ralph Golbik ◽  
Johannes A. Eble ◽  
Albert Ries ◽  
Klaus Kühn
Keyword(s):  
Energy Transfer ◽  
Amino Acid ◽  
Fluorescence Resonance Energy Transfer ◽  
Spatial Orientation ◽  
Essential Amino Acid ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Collagen Iv ◽  
Recognition Site ◽  
Amino Acid Residues

scholarly journals Measuring distances between TRPV1 and the plasma membrane using a noncanonical amino acid and transition metal ion FRET

2016 ◽  
Vol 147 (2) ◽  
pp. 201-216 ◽  
Author(s):  
William N. Zagotta ◽  
Moshe T. Gordon ◽  
Eric N. Senning ◽  
Mika A. Munari ◽  
Sharona E. Gordon
Keyword(s):  
Plasma Membrane ◽  
Energy Transfer ◽  
Amino Acid ◽  
Membrane Proteins ◽  
Transition Metal ◽  
Fluorescence Resonance Energy Transfer ◽  
Metal Ion ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Noncanonical Amino Acid

Despite recent advances, the structure and dynamics of membrane proteins in cell membranes remain elusive. We implemented transition metal ion fluorescence resonance energy transfer (tmFRET) to measure distances between sites on the N-terminal ankyrin repeat domains (ARDs) of the pain-transducing ion channel TRPV1 and the intracellular surface of the plasma membrane. To preserve the native context, we used unroofed cells, and to specifically label sites in TRPV1, we incorporated a fluorescent, noncanonical amino acid, L-ANAP. A metal chelating lipid was used to decorate the plasma membrane with high-density/high-affinity metal-binding sites. The fluorescence resonance energy transfer (FRET) efficiencies between L-ANAP in TRPV1 and Co2+ bound to the plasma membrane were consistent with the arrangement of the ARDs in recent cryoelectron microscopy structures of TRPV1. No change in tmFRET was observed with the TRPV1 agonist capsaicin. These results demonstrate the power of tmFRET for measuring structure and rearrangements of membrane proteins relative to the cell membrane.

Evaluation of a D-amino-acid-containing fluorescence resonance energy transfer peptide library for profiling prokaryotic proteases

2013 ◽  
Vol 441 (1) ◽  
pp. 38-43 ◽  
Author(s):  
Wendy E. Kaman ◽  
Ingrid Voskamp-Visser ◽  
Denise M.C. de Jongh ◽  
Hubert P. Endtz ◽  
Alex van Belkum ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Amino Acid ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Peptide Library ◽  
Fluorescence Resonance
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