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Understanding the Interactions Between γ‐B Crystallins
Author(s) -
Melake Abigail,
Fraser Olivia,
Fadden Aaron,
Faraone Julia,
Williams Zach,
Mills Jeffrey,
Thurston George,
Michel Lea Vacca
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.01809
Subject(s) - crystallin , protein aggregation , nuclear magnetic resonance spectroscopy , chemistry , biophysics , protein–protein interaction , biochemistry , biology , stereochemistry
The eye lens functions to focus light on the retina and is mostly composed of α, β, and γ‐crystallins, which are water‐soluble proteins. Aggregation of these proteins due to insolubility causes light to scatter, which can result in a cataract, leading to visual impairment or blindness. Aggregation of the crystallins can be due to unfavorable protein‐protein interactions. Here, we describe our analysis of some of those protein‐protein interactions using nuclear magnetic resonance (NMR) spectroscopy. Preliminary data suggest that NMR is a useful tool in exploring the detailed protein‐protein interactions between crystallins. Specifically, we used T1/T2 and DOSY NMR experiments to show that rotational and translational diffusion of bovine γ‐B crystallin proteins (homologue to human γ‐D crystallins) are affected by temperature and protein concentration and possibly changes in protein aggregation.