Are structural proteins in insect cuticles dominated by intrinsically disordered regions?

被引：19

作者：

Andersen, Svend Olav ^{[1
]}

机构：

[1] Royal Danish Acad Sci & Letters, Collstrop Fdn, DK-1553 Copenhagen V, Denmark

来源：

INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY | 2011年 / 41卷 / 08期

关键词：

R&R Consensus; alpha-Helix; beta-Strands; Disordered regions; Resilin; Predictors; SECONDARY STRUCTURE PREDICTION; ARTHROPOD CUTICULAR PROTEINS; UNSTRUCTURED REGIONS; SOFT-CUTICLE; RESILIN; LOCUST; ELASTICITY; CONSENSUS; FEATURES; DOMAIN;

D O I：

10.1016/j.ibmb.2011.03.015

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：

Fifty years ago it was concluded that the highly elastic cuticular protein, resilin, is devoid of secondary structure and that the peptide chains are randomly coiled and easily and reversibly deformed. These properties indicate that resilin is an intrinsically disordered protein and suggest that also other cuticular proteins may contain disordered regions. Amino acid sequences are now available for cuticular proteins from many insect species, and several programs have been developed to predict the probability for a given protein to contain disordered regions. The present paper describes the results obtained when the predictors are applied to various types of cuticular proteins from several insects. The results suggest that most cuticular proteins contain shorter or longer disordered regions, and the possible functions for such regions are briefly discussed. (C) 2011 Elsevier Ltd. All rights reserved.

引用

页码：620 / 627

页数：8

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