Characterization of different-sized human αA-crystallin homomers and implications to Asp151 isomeriz...
Characterization of different-sized human αA-crystallin homomers and implications to Asp151 isomerization
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Publisher
United States: Public Library of Science
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Language
English
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Publisher
United States: Public Library of Science
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Scope and Contents
Contents
Site-specific modifications of aspartate residues spontaneously occur in crystallin, the major protein in the lens. One of the primary modification sites is Asp151 in αA-crystallin. Isomerization and racemization alter the crystallin backbone structure, reducing its stability by inducing abnormal crystallin–crystallin interactions and ultimately le...
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Full title
Characterization of different-sized human αA-crystallin homomers and implications to Asp151 isomerization
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TN_cdi_plos_journals_3078994750
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_3078994750
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ISSN
1932-6203
E-ISSN
1932-6203
DOI
10.1371/journal.pone.0306856
