Hydrophobicity and flexibility of αA- and αB-crystallin are different
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,General Medicine,Biochemistry,Structural Biology
Reference73 articles.
1. αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues
2. Expression of the murine alpha B-crystallin gene is not restricted to the lens.
3. Cellular distribution of alpha B-crystallin in non-lenticular tissues.
4. Immunoreactive αA crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method
5. Toxic effects of high levels of ppGpp in Escherichia coli are relieved by rpoB mutations.
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2. Temperature Effects on Structural and Functional Properties of Rat Lens Phe71 Mutant αA-Crystallins;Journal of the Chinese Chemical Society;2008-10
3. Structural and Functional Roles of Deamidation and/or Truncation of N- or C-Termini in Human αA-Crystallin;Biochemistry;2008-08-29
4. Differences in properties between human αA- and αB-crystallin proteins expressed in Escherichia coli cells in response to cold and extreme pH;Biochemical Journal;2003-10-15
5. Effect of trifluoroethanol on the structural and functional properties of alpha-crystallin;Journal of Protein Chemistry;2002
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