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蛋白酶解数据库:通过蛋白质裂解计算确定α-糜蛋白酶的特异性

Proteolysis Data Bank: specificity of alpha-chymotrypsin from computation of protein cleavages.

作者信息

Keil B

机构信息

Unité de Chimie des Proteines, Institut Pasteur, Paris, France.

出版信息

Protein Seq Data Anal. 1987;1(1):13-20.

PMID:3447153
Abstract

The specificity of alpha-chymotrypsin was determined by computation of data retrieved from the Proteolysis Data Bank. The coefficients Kn enable the calculation of the relative influence of the neighbouring amino acid residues in subsites P3--P'3 on the probability of cleavage of polypeptide substrates. The extent of the fixation sites of chymotrypsin and pepsin are compared. The results of the study indicate that predictions of cleavage by proteolytic enzymes can be made from the sequence of polypeptide substrates, provided that a sufficient pool of experimental data has been collected.

摘要

通过计算从蛋白水解数据库检索到的数据,确定了α-糜蛋白酶的特异性。系数Kn能够计算亚位点P3--P'3中相邻氨基酸残基对多肽底物裂解概率的相对影响。比较了糜蛋白酶和胃蛋白酶的固定位点范围。研究结果表明,只要收集了足够的实验数据池,就可以从多肽底物序列预测蛋白水解酶的裂解情况。

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