作者: Richard A. Paselk , Daniel Levy
DOI: 10.1016/0005-2795(76)90085-4
关键词:
摘要: Abstract 19F nuclear magnetic resonance spectroscopy has been used to study the effects of salts and denaturants on structure aggregation properties several trifluoroacetyl derivatives insulin. This technique shown be a powerful tool in specific sites protein molecule. Circular dichroic sedimentation velocity studies were also carried out aid interpretation data. At pH 6.8 Zn2+ had no effect spectrum, however, citrate acetate ions significantly sharpened signal from probe at N-terminal end (glycineA-1) insulin A chain. No alterations observed S20,w value or circular spectra, suggesting that gained considerable degree motional freedom without changes conformational properties. In absence perturbants group glycineA-1 showed considerably more than phenylalanineB-1. Guanidine hydrochloride sodium dodecyl sulfate unfolding trifluoroacetylinsulin derivatives. The results suggested differential environments probes located glycineA-1, phenylalanineB-1, lysineB-29 molecule as concentration perturbant was increased.