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• W1970762912 abstract "α‐and βB2Crystallin are the major proteins in the mammalian lens. Each of these crystallins has short, flexible terminal extensions from its domain core; the two α‐crystallin subunits have C ‐terminal extensions of eight and ten amino acids whilst βB2‐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 1 H NMR spectroscopy, The N ‐terminal extension of βB2‐crystallin and the C ‐terminal extensions of α‐crystallin adopt little ordered structure. In the membrane‐mimicking solvent trifluoroethanol, the α‐crystallin extensions are also unstructured. In contrast, the C ‐terminal extension of βB2‐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 βB2‐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 βB2‐crystallin may therefore have implications for the role of this extension in crystallin‐crystallin interactions. ©Munksgaard 1996." @default.
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• W1970762912 date "1996-01-01" @default.
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• W1970762912 title "Solution conformation of bovine lens α-and βB2-crystallin terminal extensions" @default.
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• W1970762912 doi "https://doi.org/10.1111/j.1399-3011.1996.tb00804.x" @default.
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