Endothelin 1: conformation and aggregation.
The features of the far UV CD spectrum of endothelin 1 (ET 1) in water-containing solutions rules out the presence of any alpha-helical contribution, thus questioning the conclusions made by several authors on the basis of NMR investigations. We propose here a structural model, based on a succession of beta turns, which is consistent with both the NMR and the CD data. Using electron microscopy, we show that ET 1 can form "micelles," and the micelles self-associate into percolation clusters which have a fractal dimension of 1.23 in a 2D space. These data, too, are in agreement with our proposed structural model.
Calas
B
B
CNRS-INSERM, Montpellier, France.
Harricane
M C
MC
Guimard
L
L
Heitz
F
F
Mendre
C
C
Chabrier
P E
PE
Bennes
R
R
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D016232:Endothelins / Q000737:chemistry*; D008854:Microscopy, Electron; D008961:Models, Structural; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012996:Solutions
D016232:Endothelins; D012996:Solutions