REFOLD: An analytical database of protein refolding methods

被引:25
作者
Chow, MKM
Amin, AA
Fulton, KF
Whisstock, JC
Buckle, AM
Bottomley, SP
机构
[1] Monash Univ, Dept Biochem & Mol Biol, Clayton, Vic 3800, Australia
[2] Monash Univ, Victorian Bioinformat Consortium, Clayton, Vic 3800, Australia
[3] Monash Univ, ARC Ctr Struct & Funct Microbial Genom, Clayton, Vic 3800, Australia
基金
英国医学研究理事会;
关键词
inclusion bodies; protein refolding; renaturation; database;
D O I
10.1016/j.pep.2005.07.022
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The expression and harvesting of proteins from insoluble inclusion bodies by solubilization and refolding is a technique commonly used in the production of recombinant proteins. To bring clarity to the large and widespread quantity of published protein refolding data, we have recently established the REFOLD database (http://refold.med.monash.edu.au), which is a freely available, open repository for protocols describing the refolding and purification of recombinant proteins. Refolding methods are currently published in many different formats and resources-REFOLD provides a standardized system for the structured reporting and presentation of these data. Furthermore, data in REFOLD are readily accessible using a simple search function, and the database also enables analyses which identify and highlight particular trends between suitable refolding and purification conditions and specific protein properties. This information may in turn serve to facilitate the rational design and development of new refolding protocols for novel proteins. There are approximately 200 proteins currently listed in REFOLD, and it is anticipated that with the continued contribution of data by researchers this number will grow significantly, thus strengthening the emerging trends and patterns and making this database a valuable tool for the scientific community. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:166 / 171
页数:6
相关论文
共 16 条
[1]  
Apweiler R, 2004, NUCLEIC ACIDS RES, V32, pD115, DOI [10.1093/nar/gkw1099, 10.1093/nar/gkh131]
[2]   In vitro folding, functional characterization, and disulfide pattern of the extracellular domain of human GLP-1 receptor [J].
Bazarsuren, A ;
Grauschopf, U ;
Wozny, M ;
Reusch, D ;
Hoffmann, E ;
Schaefer, W ;
Panzner, S ;
Rudolph, R .
BIOPHYSICAL CHEMISTRY, 2002, 96 (2-3) :305-318
[3]   The matrix refolded [J].
Buckle, AM ;
Devlin, GL ;
Jodun, RA ;
Fulton, KF ;
Faux, N ;
Whisstock, JC ;
Bottomley, SP .
NATURE METHODS, 2005, 2 (01) :3-3
[4]  
Cabrita Lisa D, 2004, Biotechnol Annu Rev, V10, P31, DOI 10.1016/S1387-2656(04)10002-1
[5]  
Clark EDB, 1998, CURR OPIN BIOTECH, V9, P157
[6]   The solubility and stability of recombinant proteins are increased by their fusion to NusA [J].
De Marco, V ;
Stier, G ;
Blandin, S ;
de Marco, A .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2004, 322 (03) :766-771
[7]   Production of soluble mammalian proteins in Escherichia coli:: identification of protein features that correlate with successful expression -: art. no. 32 [J].
Dyson, MR ;
Shadbolt, SP ;
Vincent, KJ ;
Perera, RL ;
McCafferty, J .
BMC BIOTECHNOLOGY, 2004, 4 (1)
[8]  
Fahnert B, 2004, ADV BIOCHEM ENG BIOT, V89, P93
[9]   Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused [J].
Kapust, RB ;
Waugh, DS .
PROTEIN SCIENCE, 1999, 8 (08) :1668-1674
[10]   Preparative protein refolding [J].
Middelberg, APJ .
TRENDS IN BIOTECHNOLOGY, 2002, 20 (10) :437-443