当前位置:
X-MOL 学术
›
Bioorgan. Chem.
›
论文详情
Our official English website, www.x-mol.net, welcomes your
feedback! (Note: you will need to create a separate account there.)
Helix stabilization by stapled N-capping box.
Bioorganic Chemistry ( IF 4.5 ) Pub Date : 2020-06-17 , DOI: 10.1016/j.bioorg.2020.104024 Thanh K Pham 1 , Young-Woo Kim 1
中文翻译:
通过装订的N盖盒稳定螺旋。
更新日期:2020-07-03
Bioorganic Chemistry ( IF 4.5 ) Pub Date : 2020-06-17 , DOI: 10.1016/j.bioorg.2020.104024 Thanh K Pham 1 , Young-Woo Kim 1
Affiliation
The N-capping box is a distinct helix-stabilizing motif frequently found in proteins. In this study, we examined a ruthenium-mediated intramolecular backbone to side chain macrocyclization as a rigidified mimicry of the N-capping box. Experimental data indicate that the 15-membered macrocycle formed by a hept-4-enoyl staple, which directly tethers the α-amino group of N1 residue and the α-carbon of N3 residue, is highly effective in stabilizing helical structures of short peptides.
中文翻译:
通过装订的N盖盒稳定螺旋。
N上限框是蛋白质中常见的独特的螺旋稳定基序。在这项研究中,我们研究了钌介导的分子内骨架到侧链的大环化,作为N帽盒的刚性模拟。实验数据表明,直接将N1残基的α-氨基和N3残基的α-碳拴在一起的庚4-烯丙基短钉形成的15元大环在稳定短肽的螺旋结构方面非常有效。