Identification by 1H NMR spectroscopy of flexible C-terminal extensions in bovine lens α-crystallin

FEBS Letters

Volumn 311, Issue 2, 1992, Pages 143-149

  Carver, John A ^a   Aquilina, J Andrew ^a   Truscott, Roger J W ^a   Ralston, Gregory B ^b  

^a UNIVERSITY OF WOLLONGONG   (Australia)

^b UNIVERSITY OF SYDNEY   (Australia)

Author keywords

Aggregation; Conformation; Crystallin; Lens; NMR

Indexed keywords

CRYSTALLIN; ALPHA CRYSTALLIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CATTLE; CHEMISTRY; MOLECULAR GENETICS; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; ANIMAL TISSUE; LENS; NONHUMAN; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE;

AMINO ACID SEQUENCE; ANIMAL; CATTLE; CRYSTALLINS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PROTEIN CONFORMATION; SUPPORT, NON-U.S. GOV'T;

EID: 0026612249     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(92)81386-Z     Document Type: Article

References (31)

1. Calf lens α-crystallin quaternary structure
2. A possible structure for α-crystallin
3. Detection of internal motions in oligosaccharides by 1H relaxation measurements at different magnetic fields.