Peptide scanning-based identification of regions of γ-II crystallin involved in thermal aggregation: Evidence of the involvement of structurally analogous, helix-containing loops from the two double Greek key domains of the molecule
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference20 articles.
1. The distribution of the soluble proteins in the calf lens
2. Effect of change in concentration upon lens turbidity as predicted by the random fluctuation theory
3. Short-range order of crystallin proteins accounts for eye lens transparency
4. An insight into domain structures and thermal stability of gamma-crystallins.
5. STRUCTURE AND STABILITY OF γ-CRYSTALLINS-IV. AGGREGATION AND STRUCTURAL DESTABILIZATION IN PHOTOSENSITIZED REACTIONS
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