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[利用氚标记研究蛋白质的三维结构。I. 游离氨基酸作为未折叠多肽链中残基的模型]

[Study of three-dimensional structure of proteins by means of tritium labeling. I. Free amino acids as a model of residues in an unfolded polypeptide chain].

作者信息

Baratova L A, Gol'danskiĭ V I, Rumiantsev Iu M, Unukovich M S, Shiskov A V

出版信息

Mol Biol (Mosk). 1982 Jan-Feb;16(1):117-22.

PMID:7070372
Abstract

Probabilities of the incorporation of tritium label into various amino acids with alanine as a standard have been determined by "bombing" solid targets with a 3H-atom beam (2 000 K). The results show that amino acids can be used with sufficient accuracy as models of amino acid residues in a polypeptide chain under 100%, accessibility. The resulting coefficients, if taken into consideration in the analysis of intramolecular distribution of tritium in short tryptic peptides of TMV protein, will yield an equiprobable distribution in the case when the label has been introduced into a peptide. The distribution is not uniform, however, if a labelled peptide has been isolated from an "irradiated" hydrolysate protein.

摘要

通过用3H原子束(2000K)“轰击”固体靶,以丙氨酸为标准,测定了氚标记掺入各种氨基酸的概率。结果表明,在100%可及性条件下,氨基酸可作为多肽链中氨基酸残基的模型,具有足够的准确性。如果在分析烟草花叶病毒(TMV)蛋白质的短胰蛋白酶肽中氚的分子内分布时考虑所得系数,当标记引入肽中时,将产生等概率分布。然而,如果从“辐照”水解产物蛋白质中分离出标记肽,则分布并不均匀。

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