ArticlePLoS computational biology2009
Influence of sequence changes and environment on intrinsically disordered proteins.
Article in PLoS computational biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Lipid Composition Modulates Secondary Structure at the Biocondensate-Membrane Interface.bioRxiv : the preprint server for biology · 2026Article
- Functions of prolyl hydroxylation in elastin.The Journal of biological chemistry · 2026Article
- An Interpretable Machine-Learning Algorithm to Predict Disordered Protein Phase Separation Based on Biophysical Interactions.Biomolecules · 2022Article
- Critical assessment of protein intrinsic disorder prediction.Nature methods · 2021Article
- Effects of pH on an IDP conformational ensemble explored by molecular dynamics simulation.Biophysical chemistry · 2021Article
- The Effects of Chain Length on the Structural Properties of Intrinsically Disordered Proteins in Concentrated Solutions.The journal of physical chemistry. B · 2020Article
- Exploring conformational preferences of proteins: ionic liquid effects on the energy landscape of avidin.Chemical science · 2020Article
- The ortholog conjecture revisited: the value of orthologs and paralogs in function prediction.Bioinformatics (Oxford, England) · 2020Article
- Experimentally Determined Long Intrinsically Disordered Protein Regions Are Now Abundant in the Protein Data Bank.International journal of molecular sciences · 2020Article
- Membranes as the third genetic code.Molecular biology reports · 2020Review
- Pathogenicity and functional impact of non-frameshifting insertion/deletion variation in the human genome.PLoS computational biology · 2019Article
- Spontaneous Switching among Conformational Ensembles in Intrinsically Disordered Proteins.Biomolecules · 2019Review
- Estimating classification accuracy in positive-unlabeled learning: characterization and correction strategies.Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing · 2019Article
- Predictions of Backbone Dynamics in Intrinsically Disordered Proteins Using De Novo Fragment-Based Protein Structure Predictions.Scientific reports · 2017Article
- The Loss and Gain of Functional Amino Acid Residues Is a Common Mechanism Causing Human Inherited Disease.PLoS computational biology · 2016Article
- Protein function in precision medicine: deep understanding with machine learning.FEBS letters · 2016Review
- Disorder Prediction Methods, Their Applicability to Different Protein Targets and Their Usefulness for Guiding Experimental Studies.International journal of molecular sciences · 2015Review
- Missing strings of residues in protein crystal structures.Intrinsically disordered proteins · 2015Article
- Intrinsically disordered regions in autophagy proteins.Proteins · 2014Article
- Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.PloS one · 2014Article
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3 authors.
Funding
Abstract
Many large-scale studies on intrinsically disordered proteins are implicitly based on the structural models deposited in the Protein Data Bank. Yet, the static nature of deposited models supplies little insight into variation of protein structure and function under diverse cellular and environmental conditions. While the computational predictability of disordered regions provides practical evidence that disorder is an intrinsic property of proteins, the robustness of disordered regions to changes in sequence or environmental conditions has not been systematically studied. We analyzed intrinsically disordered regions in the same or similar proteins crystallized independently and studied their sensitivity to changes in protein sequence and parameters of crystallographic experiments. The observed changes in the existence, position, and length of disordered regions indicate that their appearance in X-ray structures dramatically depends on changes in amino acid sequence and peculiarities of the crystallographic experiment. Our study also raises general questions regarding protein evolution and the regulation of protein structure, dynamics, and function via variations in cellular and environmental conditions.
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