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  • Title: Solution conformation of bovine lens alpha- and betaB2-crystallin terminal extensions.
    Author: Le Breton ER, Carver JA.
    Journal: Int J Pept Protein Res; 1996; 47(1-2):9-19. PubMed ID: 8907494.
    Abstract:
    alpha- and betaB2-Crystallin are the major proteins in the mammalian lens. Each of these crystallins has short, flexible terminal extensions from its domain core; the two alpha-crystallin subunits have C-terminal extensions of eight and ten amino acids whilst betaB2-crystallin has N- and C-terminal extensions of 15 and 11 amino acids, respectively. The solution conformations of these chemically synthesised extensions have been examined by two-dimensional 1H NMR spectroscopy. The N-terminal extension of betaB2-crystallin and the C-terminal extensions of alpha-crystallin adopt little ordered structure. In the membrane-mimicking solvent trifluoroethanol, the alpha-crystallin extensions are also unstructured. In contrast, the C-terminal extension of betaB2-crystallin in water has a structural preference towards turn-like structures, creating a hydrophobic region involving G198, F200 and P202. In the lens, the C-terminal extension of betaB2-crystallin is the only one of these extensions that interacts to any large extent with other crystallins. The structural preference of the C-terminal extension of betaB2-crystallin may therefore have implications for the role of this extension in crystallin-crystallin interactions.
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