STRUCTURAL CHARACTERIZATION OF THE BETA-BEND RIBBON SPIRAL - CRYSTALLOGRAPHIC ANALYSIS OF 2 LONG (L-PRO-AIB)N SEQUENTIAL PEPTIDES

被引：95

作者：

DIBLASIO, B ^{[1
]}

PAVONE, V ^{[1
]}

SAVIANO, M ^{[1
]}

LOMBARDI, A ^{[1
]}

NASTRI, F ^{[1
]}

PEDONE, C ^{[1
]}

BENEDETTI, E ^{[1
]}

CRISMA, M ^{[1
]}

ANZOLIN, M ^{[1
]}

TONIOLO, C ^{[1
]}

机构：

[1] UNIV PADUA,DEPT ORGAN CHEM,CNR,BIOPOLYMER RES CTR,I-35131 PADUA,ITALY

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 1992年 / 114卷 / 16期

关键词：

D O I：

10.1021/ja00042a001

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The molecular and crystal structures of two terminally blocked (L-Pro-Aib)n (n = 3, 4) sequential peptides were determined by X-ray diffraction. In both crystals two molecules in the asymmetric unit are found. Either molecule in the asymmetric unit of each structure shows a right-handed beta-bend ribbon spiral, stabilized by the maximum possible number of intramolecular N-H...O=C H-bonds. Thus, for the first time it was possible to characterize at atomic resolution this polypeptide conformation.

引用

页码：6273 / 6278

页数：6

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