Supplemental material
Journal of Biomolecular Structure and Dynamics
Volume 36, 2018 - Issue 16
Research Article
Sequence fingerprints distinguish erroneous from correct predictions of intrinsically disordered protein regions
Konda Mani SaravananCentre of Advanced Study in Crystallography & Biophysics, University of Madras, Guindy Campus, Chennai600 025, Tamilnadu, India
http://orcid.org/0000-0002-5541-234X
http://orcid.org/0000-0002-5541-234X, & Sankaran KrishnaswamyInstitute of Mathematical Sciences, CIT Campus, Tharamani, Chennai600 113, Tamilnadu, IndiaCorrespondence[email protected]
http://orcid.org/0000-0002-6797-4614
http://orcid.org/0000-0002-6797-4614Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related Research Data
Comprehensive Comparative Assessment of In-Silico Predictors of Disordered Regions
Source:
Bentham Science Publishers Ltd.
MobiDB: a comprehensive database of intrinsic protein disorder annotations
Source:
Oxford University Press (OUP)
Intrinsic Disorder in the Human Spliceosomal Proteome
Source:
Public Library of Science (PLoS)
Evolutionary Rate Heterogeneity in Proteins with Long Disordered Regions
Source:
Springer Nature
Intrinsically Disordered Loops Inserted into the Structural Domains of Human Proteins
Source:
Elsevier BV
Reduced amino acid alphabet is sufficient to accurately recognize intrinsically disordered protein
Source:
Wiley
Dihedral angle preferences of amino acid residues forming various non-local interactions in proteins
Source:
Springer Nature
Association Between Foldability and Aggregation Propensity in Small Disulfide-Rich Proteins
Source:
Mary Ann Liebert Inc
POODLE-S
Source:
Oxford University Press (OUP)
Distribution and cluster analysis of predicted intrinsically disordered protein Pfam domains
Source:
Informa UK Limited
Malleable Machines in Transcription Regulation: The Mediator Complex
Source:
Public Library of Science (PLoS)
Prediction of protein disorder at the domain level.
Source:
Bentham Science Publishers Ltd.
Intrinsically disordered proteins as crucial constituents of cellular aqueous two phase systems and coacervates
Source:
Wiley
Back to the Future: Nuclear Magnetic Resonance and Bioinformatics Studies on Intrinsically Disordered Proteins
Source:
Springer International Publishing
Conservation of intrinsic disorder in protein domains and families: I. A database of conserved predicted disordered regions.
Source:
American Chemical Society (ACS)
Molecular recognition features (MoRFs) in three domains of life
Source:
Royal Society of Chemistry (RSC)
pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins
Source:
Oxford University Press (OUP)
Intrinsically disordered proteins and intrinsically disordered protein regions.
Source:
Annual Reviews
Protein disorder—a breakthrough invention of evolution?
Source:
Elsevier BV
Sequence fingerprints distinguish erroneous from correct predictions of intrinsically disordered protein regions
Source:
Figshare
IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
Source:
Oxford University Press (OUP)
Markov Models of Amino Acid Substitution to Study Proteins with Intrinsically Disordered Regions
Source:
Public Library of Science (PLoS)
Intrinsic Disorder and Functional Proteomics
Source:
Elsevier BV
ESpritz: accurate and fast prediction of protein disorder.
Source:
Oxford University Press (OUP)
Composition Profiler: a tool for discovery and visualization of amino acid composition differences
Source:
eScholarship, University of California
Assessment of protein disorder region predictions in CASP10
Source:
Wiley-Blackwell
Protein Disorder Prediction: Implications for Structural Proteomics
Source:
Elsevier BV
PrDOS: prediction of disordered protein regions from amino acid sequence
Source:
Oxford University Press (OUP)
Functional fragments of disorder in outer membrane β barrel proteins
Source:
Informa UK Limited
Inferring function using patterns of native disorder in proteins
Source:
Public Library of Science (PLoS)
DisProt: the Database of Disordered Proteins
Source:
Oxford University Press (OUP)
Intrinsically unstructured proteins and their functions.
Source:
Springer Science and Business Media LLC
Analysis of dihedral angle preferences for alanine and glycine residues in alpha and beta transmembrane regions
Source:
Informa UK Limited
A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome.
Source:
Springer Science and Business Media LLC
The Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules
Source:
Elsevier BV
:{unav)
Source:
Wiley
PONDR-FIT: a meta-predictor of intrinsically disordered amino acids.
Source:
Elsevier BV
Inferring function using patterns of native disorder in proteins
Source:
Public Library of Science (PLoS)
II. Various roles of glutamic acid in ordered and intrinsically disordered proteins
Source:
Informa UK Limited
Improved performance in protein secondary structure prediction by inhomogeneous score combination
Source:
Oxford University Press (OUP)
Prediction and functional analysis of native disorder in proteins from the three kingdoms of life.
Source:
Elsevier BV
CSSP(Consensus Secondary Structure Prediction): a web-based server for structural biologists
Source:
International Union of Crystallography (IUCr)
Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life
Source:
Informa UK Limited
Systems-wide Identification of cis-Regulatory Elements in Proteins
Source:
Elsevier BV
Intrinsically disordered protein
Source:
Elsevier BV
SCOP: A structural classification of proteins database for the investigation of sequences and structures
Source:
Elsevier BV
MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins
Source:
Oxford University Press (OUP)
Intrinsically unstructured proteins
Source:
Elsevier BV
Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome
Source:
PeerJ
Proteins: Structure, Function, and Bioinformatics
Source:
Wiley
Predicting intrinsic disorder in proteins: an overview.
Source:
Springer Science and Business Media LLC
Linking provided by
