Differences in solution dynamics between lens β-crystallin homodimers and heterodimers probed by hydrogen–deuterium exchange and deamidation - Lampi, Kirsten J.; Murray, Matthew R.; Peterson, Matthew P.; Eng, Bryce S.; Yue, Eileen; Clark, Alice R.; Barbar, Elisar; David, Larry L. (Biochimica et biophysica acta, 2016)
Keywords: 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