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Protein folding: Requirement for simulations on the basis of sequential growth of polypeptides

Mahmud A.Basharov


To solve the problemof protein folding, denaturation-renaturation experiments on native proteins and a variety of theoretical-computational simulations of full-length polypeptide chains have usually been used as convenient in vitro models for the past several decades. However, there is a lot of irrefutable evidence that the information contained in the primary structure of a protein about its spatial structure is realized in the cells during the residue-by-residue elongation on the ribosome from the N- to the C-terminus. On this basis therefore, simulations of the folding and formation of the native spatial structure of proteinswill be of requirement.


索引于

  • 中国社会科学院
  • 谷歌学术
  • 打开 J 门
  • 中国知网(CNKI)
  • 引用因子
  • 宇宙IF
  • 电子期刊图书馆
  • 研究期刊索引目录 (DRJI)
  • 秘密搜索引擎实验室
  • ICMJE

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