The structure of a filamin molecule has been studied by circular dichroism, infrared spectroscopy, scanning microcalorimetry and the inherent fluorescence of the tryptophan residues. It has been shown that the secondary structure of filamin is formed exclusively by the β form (50%); the filamin molecule consists of several domains. Some of the tryptophan residues in filamin are buried in the interior of the protein structure, whereas others are located on the surface of the filamin molecule. These results, as well as the data of previous reports, suggest the following description of the filamin molecule : the protein molecule is highly assymetric and elongated consisting of structural domains with a β-form structure interconnected by flexible regions of the polypeptide chain.
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Koteliansky et al. (1982) studied this question.
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