作者: Rachel W. Martin
DOI: 10.1002/9780470034590.EMRSTM1354
关键词: Magic angle spinning 、 Eye Lens Protein 、 Chemistry 、 Intermolecular force 、 Crystallin 、 Biochemistry 、 Chaperone (protein) 、 Eye lens 、 Solubility 、 Chemical modification
摘要: The crystallins of the eye lens are highly stable, soluble proteins that generate refractive index gradient lens. In their native context, form large oligomers; a loss in solubility due to mutation, UV light damage, or chemical modification results cataract. There two broad classes ubiquitous crystallin proteins; βγ-crystallins, which purely structural, and α-crystallins, additionally play chaperone role, maintaining compromised NMR methods have been used investigate many structural functional properties both types crystallins. Structures solved for using solid-state solution NMRs, these detailed molecular pictures as starting point investigating conformational dynamics intermolecular interactions. Keywords: crystallin; eye protein; small heat-shock protein; molecular chaperone; solution-state ; magic angle spinning