Suppr超能文献

各种肽与钙调蛋白的相互作用。

Interaction of various peptides with calmodulin.

作者信息

Sellinger-Barnette M, Weiss B

出版信息

Adv Cyclic Nucleotide Protein Phosphorylation Res. 1984;16:261-76.

PMID:6326527
Abstract

In summary, we have demonstrated the existence of several endogenous substances capable of inhibiting the action of calmodulin and have identified certain structural features of a peptide that confer calmodulin inhibitory activity. These include a net positive charge, a region of hydrophobic amino acids, and the ability to form a hydrophobic alpha-helix. We believe that these properties can be used to predict the calmodulin inhibitory potency of other peptides and can also provide an insight into the structural characteristics present in calmodulin-sensitive enzymes.

摘要

总之,我们已经证明了几种能够抑制钙调蛋白作用的内源性物质的存在,并确定了赋予钙调蛋白抑制活性的肽的某些结构特征。这些特征包括净正电荷、疏水氨基酸区域以及形成疏水α螺旋的能力。我们认为,这些特性可用于预测其他肽的钙调蛋白抑制效力,还能深入了解钙调蛋白敏感酶中存在的结构特征。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验