ArticlePLoS computational biology2006
Wiggle-predicting functionally flexible regions from primary sequence.
Article in PLoS computational biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Who cites it
15 citing papers in PubMed.
- Splice junctions are constrained by protein disorder.Nucleic acids research · 2015Article
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- Prediction of protein motions from amino acid sequence and its application to protein-protein interaction.BMC structural biology · 2010Article
- Understanding protein non-folding.Biochimica et biophysica acta · 2010Review
- Protein secondary structure appears to be robust under in silico evolution while protein disorder appears not to be.Bioinformatics (Oxford, England) · 2010Article
- Calling International Rescue: knowledge lost in literature and data landslide!The Biochemical journal · 2009Review
- Analytical methods for inferring functional effects of single base pair substitutions in human cancers.Human genetics · 2009Review
- Article
- Interaction between the C-terminal region of human myelin basic protein and calmodulin: analysis of complex formation and solution structure.BMC structural biology · 2008Article
- FlexPred: a web-server for predicting residue positions involved in conformational switches in proteins.Bioinformation · 2008Article
- Natively unstructured loops differ from other loops.PLoS computational biology · 2007Article
- Prediction of flexible/rigid regions from protein sequences using k-spaced amino acid pairs.BMC structural biology · 2007Article
- Intrinsic disorder and functional proteomics.Biophysical journal · 2007Review
- Identifying allosteric fluctuation transitions between different protein conformational states as applied to Cyclin Dependent Kinase 2.BMC bioinformatics · 2007Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The Wiggle series are support vector machine-based predictors that identify regions of functional flexibility using only protein sequence information. Functionally flexible regions are defined as regions that can adopt different conformational states and are assumed to be necessary for bioactivity. Many advances have been made in understanding the relationship between protein sequence and structure. This work contributes to those efforts by making strides to understand the relationship between protein sequence and flexibility. A coarse-grained protein dynamic modeling approach was used to generate the dataset required for support vector machine training. We define our regions of interest based on the participation of residues in correlated large-scale fluctuations. Even with this structure-based approach to computationally define regions of functional flexibility, predictors successfully extract sequence-flexibility relationships that have been experimentally confirmed to be functionally important. Thus, a sequence-based tool to identify flexible regions important for protein function has been created. The ability to identify functional flexibility using a sequence based approach complements structure-based definitions and will be especially useful for the large majority of proteins with unknown structures. The methodology offers promise to identify structural genomics targets amenable to crystallization and the possibility to engineer more flexible or rigid regions within proteins to modify their bioactivity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.