Paper Info
Title
Globplot: Exploring Protein Sequences For Globularity And Disorder
Abstract
A major challenge in the proteomics and structural genomics era is to predict protein structure and function, including identification of those proteins that are partially or wholly unstructured. Non-globular sequence segments often contain short linear peptide motifs (e.g. SH3-binding sites) which are important for protein function. We present here a new tool for discovery of such unstructured, or disordered regions within proteins. GlobPlot (http://globplot.embl.de) is a web service that allows the user to plot the tendency within the query protein for order/globularity and disorder. We show examples with known proteins where it successfully identifies inter-domain segments containing linear motifs, and also apparently ordered regions that do not contain any recognised domain. GlobPlot may be useful in domain hunting efforts. The plots indicate that instances of known domains may often contain additional N- or C-terminal segments that appear ordered. Thus GlobPlot may be of use in the design of constructs corresponding to globular proteins, as needed for many biochemical studies, particularly structural biology. GlobPlot has a pipeline interface-GlobPipe-for the advanced user to do whole proteome analysis. GlobPlot can also be used as a generic infrastructure package for graphical displaying of any possible propensity.
Year
DOI
Venue
2003
10.1093/nar/gkg519
NUCLEIC ACIDS RESEARCH
Keywords
Field
DocType
computer graphics,protein structure,binding site,protein sequence,internet,algorithms,web service,structural biology,proteome,structural genomics
Structural genomics,Short linear motif,Biology,Proteomics,Structural biology,Globular protein,Genomics,Proteome,Molecular biology,Protein structure
Journal
Volume
Issue
ISSN
31
13
0305-1048
Citations 
PageRank 
References 
90
10.20
12
Authors
4
Name
Order
Citations
PageRank
Rune Linding129430.01
Robert B Russell246536.01
Victor Neduva311612.39
Toby J. Gibson41210211.39