Polyproline helices in protein structures: A statistical survey

被引：37

作者：

Berisio, Rita

Loguercio, Salvatore

De Simone, Alfonso

Zagari, Adriana

Vitagliano, Luigi

机构：

[1] CNR, Ist Biostruct & Bioimmagini, I-80134 Naples, Italy

[2] Univ Naples Federico II, Sez Biostruct, Dipartimento Sci Biol, I-80134 Naples, Italy

[3] CNISM, I-80125 Naples, Italy

[4] CIRPEB, I-80134 Naples, Italy

来源：

PROTEIN AND PEPTIDE LETTERS | 2006年 / 13卷 / 08期

关键词：

PPII helices; collagen; imino-acids; statistical survey; bioinformatics;

D O I：

10.2174/092986606777841154

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

A statistical survey of polyproline II (PPII) helices extracted from protein crystal structures is here reported. The average hydrophobicity of these helices is intermediate between those displayed by beta-strands and coil regions and is similar to that of alpha-helices. PPII helices with amphipathic properties have been identified and classified. Amino acid propensities for PPII helices derived in this study differ significantly from those previously reported. They show a little albeit significant correlation with propensities for alpha-helices whereas they are fully non-correlated to propensities for beta-sheets. Finally, PPII propensities have been correlated with amino acid frequencies in structural proteins, such as collagen and extensins.

引用

页码：847 / 854

页数：8

共 44 条

[1]

LEFT-HANDED POLYPROLINE-II HELICES COMMONLY OCCUR IN GLOBULAR-PROTEINS [J].