摘要
根据PDB提供的PrPC 的原子坐标 ,利用MSMS程序 ,对PrPC 氨基酸残基溶剂可及表面积进行了计算和分析。结果表明 :(1)PrPC 氨基酸残基可及性具有总体一致性特点 ;(2 )PrPC 蛋白质序列中非保守残基与种间屏障有一定关系 ;(3)在PrPC 向PrPSc转变过程中 ,由于蛋白质X的结合 ,PrPC 可能会出现一定的构象变化 ,这种变化利于PrPC 向PrPSc发生转变。
According to the atom's coordinate of prion protein amino acid residues from the PDB, we calculated and discussed the ASA of amino acid residues of prion protein using MSMS program. Results indicated: (1) the accessibility of PrPC amino acid residues had the characteristic of total consistency; (2) there was certain relation between the nonconservative residues of PrPC sequence and species barrier; (3) in the course of PrPC inverting into PrP Sc, because of the combination with protein X, PrPC may occur some conformational invertion , and it may benefit the transformation of PrPC to PrP Sc.
出处
《氨基酸和生物资源》
CAS
2003年第4期28-32,共5页
Amino Acids & Biotic Resources
基金
自然科学基金资助项目 (项目批准号 :3 0 3 70 0 5 4)
