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

Research output: Chapter in Book/Report/Conference proceedingChapter


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.

Original languageEnglish (US)
Title of host publicationHuman Cataract Formation
Number of pages18
ISBN (Electronic)9780470720875
ISBN (Print)0272797758, 9780272797754
StatePublished - May 30 2008
Externally publishedYes


  • Degree of water retention
  • Molecular models
  • Molecular structures
  • Protein aggregation in cataract
  • Thermodynamic stability

ASJC Scopus subject areas

  • Medicine(all)


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