Abstract
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 language | English (US) |
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Title of host publication | Human Cataract Formation |
Publisher | Wiley-Blackwell |
Pages | 219-236 |
Number of pages | 18 |
ISBN (Electronic) | 9780470720875 |
ISBN (Print) | 0272797758, 9780272797754 |
DOIs | |
State | Published - May 30 2008 |
Externally published | Yes |
Keywords
- Degree of water retention
- Molecular models
- Molecular structures
- Protein aggregation in cataract
- Thermodynamic stability
ASJC Scopus subject areas
- General Medicine