Differences in solution dynamics between lens β-crystallin homodimers and heterodimers probed by hydrogen–deuterium exchange and deamidation

• Published in: Biochimica et biophysica acta Vol. 1860; no. 1; pp. 304 - 314
• Main Authors: Lampi, Kirsten J., Murray, Matthew R., Peterson, Matthew P., Eng, Bryce S., Yue, Eileen, Clark, Alice R., Barbar, Elisar, David, Larry L.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.01.2016
• Subjects: Amides - chemistry; Amino Acid Sequence; Animals; beta-Crystallins - chemistry; beta-Crystallins - ultrastructure; Binding Sites; cataract; Cataracts; crosslinking; crystallins; Deamidation; deuterium; Deuterium Exchange Measurement - methods; Dimerization; eye lens; heat stability; Humans; Hydrogen–deuterium exchange; Lens; Lens, Crystalline - chemistry; Mass spectrometry; Molecular Probe Techniques; Molecular Sequence Data; peptides; Protein Binding; Protein Conformation; Protein Multimerization; Solution dynamics; solvents; structural proteins; β-Crystallins; Cataracts; Solution dynamics; Hydrogen–deuterium exchange; β-Crystallins; Deamidation; Lens; Mass spectrometry

Lens transparency is due to the ordered arrangement of the major structural proteins, called crystallins. βB2 crystallin in the lens of the eye readily forms dimers with other β-crystallin subunits, but the resulting heterodimer structures are not known and were investigated in this study. Structure...