Elucidating the Electrostatic Interactions of Bovine Gamma‐B Crystallin via Site‐Directed Mutagenesis
نویسندگان
چکیده
منابع مشابه
Enhanced crystallization of the Cys18 to Ser mutant of bovine gammaB crystallin.
The cysteine residues of the gamma crystallins, a family of ocular lens proteins, are involved in the aggregation and phase separation of these proteins. Both these phenomena are implicated in cataract formation. We have used bovine gammaB crystallin as a model system to study the role of the individual cysteine residues in the aggregation and phase separation of the gamma crystallins. Here, we...
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this thesis deals with the construction of some function algebras whose corresponding semigroup compactification are universal with respect to some properies of their enveloping semigroups. the special properties are of beigan a left zero, a left simple, a group, an inflation of the right zero, and an inflation of the rectangular band.
15 صفحه اولPrediction of stability factors at the domain interface of human gammaB crystallin maintaining the transparency of the eye lens.
OBJECTIVE betagamma-crystallins are among the most long lived globular proteins known today. Interaction of the two domains through a hydrophobic interface is one of the major contributors to the stability of these crystallins. Changes in these interactions are either due to the amino acid substitutions or the changes in the orientations of the same amino acids leading to cataract formation. We...
متن کاملAnalysis of crystallin-crystallin interactions by surface plasmon resonance.
The mechanism of aggregation and insolubilization of lens proteins was examined based on the kinetics of crystallin-crystallin interaction determined by the surface plasmon resonance method on a BlAcore system. Lens proteins are composed mainly of three types crystallins, alpha-, beta-, and gamma-crystallin. The present study indicated that alpha-crystallin shows marked self-interaction. Furthe...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2021
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.2021.35.s1.02134