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对肽链中第2位和第5位含有两个脱氢氨基酸残基的六肽的构象研究。

Conformational studies of hexapeptides containing two dehydroamino acid residues in positions 2 and 5 in peptide chain.

作者信息

Latajka Rafal, Jewginski Michal, Makowski Maciej, Krezel Artur, Paluch Slawomir

机构信息

Faculty of Chemistry, Department of Bioorganic Chemistry, Wroclaw University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland.

出版信息

Biopolymers. 2008 Aug;89(8):691-9. doi: 10.1002/bip.20994.

Abstract

Conformational preferences of a group of hexapeptides containing two dehydroamino acid residues in Positions 2 and 5 in peptide chain were investigated by means of spectroscopic methods (NMR and CD) and theoretical calculations. In the case of dimethylsulfoxide (DMSO) solution, only peptide with free N-termini adopted rigid 3(10)-helical conformation, for the rest of examined peptides extended and "zig-zag" conformers were predominant. CD measurements showed that only in chloroform solution the conformational freedom of investigated peptides was restricted.

摘要

通过光谱方法(核磁共振和圆二色光谱)和理论计算研究了一组在肽链第2位和第5位含有两个脱氢氨基酸残基的六肽的构象偏好。在二甲基亚砜(DMSO)溶液中,只有具有游离N端的肽采用刚性的3(10)-螺旋构象,其余检测的肽以伸展和“之字形”构象为主。圆二色光谱测量表明,只有在氯仿溶液中,所研究肽的构象自由度才受到限制。

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