Endothelin 1: conformation and aggregation.

B Calas; M C Harricane; L Guimard; F Heitz; C Mendre; P E Chabrier; R Bennes

PubMed · 1581643

Endothelin 1: conformation and aggregation.

B Calas·M C Harricane·L Guimard·F Heitz·C Mendre·P E Chabrier·R Bennes

Abstract

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.

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Amino Acid Sequence Circular Dichroism Endothelins Microscopy, Electron Models, Structural Molecular Sequence Data Protein Conformation Solutions Journal Article

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B Calas, M C Harricane, L Guimard, F Heitz, C Mendre, P E Chabrier, R Bennes. Endothelin 1: conformation and aggregation.. https://pubmed.ncbi.nlm.nih.gov/1581643/

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