Folded Structures in Protonated Reduced Dipeptides

被引:9
作者
Grand, Vincent [1 ,2 ]
Aubry, Andre
Dupont, Virginie [1 ,2 ]
Vicherat, Andre [1 ,2 ]
Marraud, Michel [1 ,2 ]
机构
[1] ENSIC, INPL, Lab Macromol Phys Chem, F-54001 Nancy, France
[2] Univ Nancy 1, Lab Cristallog & Modelling Mineral & Biol Mat, Vandoeuvre Les Nancy, France
关键词
conformational analysis; crystal structure; folded structures; pseudopeptides; reduced peptides;
D O I
10.1002/psc.78
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Reduced dipeptides with the general formula RCO-Xaa-rXbb-N+HR'R '' (rXbb, reduced analogue of residue Xbb: NH-(CHR1)-H-alpha-CrH2) are shown to adopt a folded conformation in solution and in the solid state. The protonated reduced amide bond is an active proton donor capable of interacting with a peptide carbonyl to give a strong hydrogen bond topologically equivalent to the i + 2 or i + 3 -> i interaction. The resulting conformation is similar to the gamma- or beta-turn structure found in peptides and proteins.
引用
收藏
页码:381 / 391
页数:11
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