新生肽链

新生肽链新生肽链
  1. 甲硫氨酸氨基肽酶负责切除新生肽链N端的起始甲硫氨酸,其编码基因是细胞存活的必需基因。

    Methionine aminopeptidase ( MAP ) is responsible for removing N-terminal methionine from nascent peptides and the gene is essential to the cell .

  2. mRNA解折叠的链构象与相应新生肽链构象相关性的探索而当湿度小于75%大于40%范围时分子的二级结构改变以β折叠和无规卷曲的肽链构象。

    The Correlation Between the Chain conformations of Unfolded mRNA and Corresponding Nascent Polypeptide R 40 % - 75 % , it can be obtained as antiparallel β - cheet and random coil conformation .

  3. 分子伴侣(molecularchaperones)是一组从细菌到人广泛存在的蛋白质,非共价地与新生肽链和解折叠的蛋白质肽链结合,并帮助它们折叠和转运,通常不参与靶蛋白的生理功能。

    The molecular chaperone ( molecular chaperones ) are a group of widespreads from bacteria to human proteins , non-covalent reconciliation with the nascent chain folding of proteins chain binding , and help them fold and transport , usually not involved in the physiological functions of target proteins .

  4. 第一类释放因子是新生肽链释放所必需的因子,它能正确地识别终止信号,水解肽酰tRNA酯键,释放出新合成的多肽链。

    The class 1 release factor is required in termination of protein synthesis . It could accurately recognize the stop signal and promotes the hydrolysis of the ester bond linking the polypeptide chain with the peptidyl ( p ) site tRNA .

  5. 新生肽链折叠的研究是解决目前蛋白质折叠研究中所遇到问题的关键。

    The research of the nascent peptide folding is the key to resolve the problems of the protein folding .

  6. 分子伴侣蛋白在生物体内的主要功能是帮助新生肽链的折叠以及防止变性蛋白的聚集等。

    New Life Molecular chaperones are predominantly involved in assisting newly synthesized protein folding and in preventing denaturing proteins from misfolding and aggregation .

  7. 这样新生肽链的合成,延伸,折叠,构象调整,直到最终三维构象的形成,是一个同时进行的,协调的动态过程。显然这与一条变性伸展的完整肽链的重折叠情况完全不同的。

    Chenglu Zou pointed out that nascent peptide folding is different from the refolding in vitro and is a simultaneously - happening process of synthesis , folding , the adjustment of the configuration .