title: ¹H, ¹³C, and ¹⁵N assignments of wild-type human γS-crystallin and its cataract-related variant γS-G18V.
abstract: We present the backbone and sidechain NMR assignments and a structural analysis of the 178-residue wild-type γS-crystallin and the cataract-related point mutant, γS-G18V. γS-crystallin is a structural component of the eye lens, which maintains its solubility and stability over many years. NMR assignments and continued structural investigations of γS-crystallin and aggregation-prone variants will advance understanding of cataract formation.
authors: Department of Molecular Biology and Biochemistry, University of California, Irvine, CA, USA.
authors: William D
authors: WD
authors: Brubaker
authors: Rachel W
authors: RW
authors: Martin
mesh_terms: D000595:Amino Acid Sequence; D002386:Cataract / Q000235:genetics*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D009154:Mutation; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D013696:Temperature; D038222:gamma-Crystallins / Q000737:chemistry* / Q000235:genetics*
chemical_list: D038222:gamma-Crystallins; C077648:CRYGS protein, human