摘要
主要报导TEM-1β-内酰胺酶的天然蛋白类抑制剂BLIP中一段多肽B1的溶液构象研究结果.在磷酸盐缓冲溶液中，通过圆二色光谱、傅立叶红外光谱和核磁共振谱研究了B1的二级结构特征.实验结果表明，B1在溶液中形成了β-转角结构，为在溶液中单独研究β-转角结构形成与稳定性提供了良好的模板.β-转角在溶液中可以独立存在，表明β-转角在蛋白质折叠过程中可能具有重要作用.
The model six-residue linear peptide AAGDYY-NH2 from TEM-1 β-lactamase inhibitor protein and BLIP was predicted to adopt a β-turn conformation and synthesized in order to elucidate the mechanism of β-turn formation and stability.Its structural preferences in solution were comprehensively characterized using CD (circular dichroism),FT-IR and 1H-NMR spectroscopy.The set of observed short-and medium-range NOEs,the restrained molecular dynamics simulation,CD and FT-IR spectroscopy were consistent with the formation of β-turn in solution by the model peptide.The results implicate β-turn playing an important role in the process of protein folding.
出处
《物理化学学报》
SCIE
CAS
CSCD
北大核心
2001年第7期619-621,共3页
Acta Physico-Chimica Sinica
基金
"九五"攀登项目资助(970211006)
