The Molecular Structures and Interactions of Bovine and Human γ-Crystallins

Lesley Summers, Christine Slingsby, Helen White, Michael Narebor, David Moss, Linda Miller, Daruka Mahadevan, Peter Lindley, Huub Driessen, Tom Den Blundell, Johan D. Dunsen, Rob Moormann, Rob Van Leen, John Schoenmakers

Producción científica: Chapter


Knowledge of the three-dimensional structure of twine γll-crystallin has provided the basis for building molecular models using computer graphics of two humanγ-crystallins. the sequences of which hase recently been determined. The tertiary structures of these γ-crystallins arc predicted to he highly conserved. They have extensive networks of interacting charges on their surfaces, which may contribute to their thermodynamic stability and partially define the degree of water retention in the lens. The human crystallins appear to be more hydrophobic than the bovine molecule. All have arrangements of cysteine thiols which may be important as electron sinks and reserve redox potential in the normal lens but which may contribute to protein aggregation in cataract.

Idioma originalEnglish (US)
Título de la publicación alojadaHuman Cataract Formation
Número de páginas18
ISBN (versión digital)9780470720875
ISBN (versión impresa)0272797758, 9780272797754
EstadoPublished - may 30 2008
Publicado de forma externa

ASJC Scopus subject areas

  • General Medicine


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