Intermolecular Interaction of Lens Crystallins: From Rotationally Mobile to Immobile States at High Protein Concentrations
- 19 May 1998
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 246 (2) , 441-445
- https://doi.org/10.1006/bbrc.1998.8640
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Intermolecular protein interactions in solutions of calf lens alpha-crystallin. Results from 1/T1 nuclear magnetic relaxation dispersion profilesBiophysical Journal, 1992
- Protein interactions in the calf eye lens: interactions between ?-crystallins are repulsive whereas in ?-crystallins they are attractiveEuropean Biophysics Journal, 1992
- Interaction and aggregation of lens crystallinsExperimental Eye Research, 1991
- Molecular basis of eye lens transparencyJournal of Molecular Biology, 1989
- Relaxometry of calf lens homogenates, including cross‐relaxation by crystallin NH groupsMagnetic Resonance in Medicine, 1988
- Preferential interaction among lens proteins as evidenced from accessibility of crystallins to ammonia gasExperimental Eye Research, 1988
- Short-range order of crystallin proteins accounts for eye lens transparencyNature, 1983
- Effect of change in concentration upon lens turbidity as predicted by the random fluctuation theoryBiophysical Journal, 1983
- Excluded volume as a determinant of macromolecular structure and reactivityBiopolymers, 1981
- Theory of Transparency of the EyeApplied Optics, 1971