Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Mutations01:39

Mutations

Overview
Mutations01:35

Mutations

Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Protein Folding01:22

Protein Folding

Overview

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Machine Learning-Based Frailty Prediction and Classification in Community-Dwelling Older Adults: A Systematic Review of Validation, Explainability, and Implementation Readiness.

Healthcare (Basel, Switzerland)·2026
Same author

GeoFusion-3D: Multi-Scale Geomorphic Feature Fusion for Landslide Scar Detection Using UAV-Mounted LiDAR.

Sensors (Basel, Switzerland)·2026
Same author

Development of machine learning models with explainable AI for frailty risk prediction and their web-based application in community public health.

Frontiers in public health·2025
Same author

A Cross-Sectional Social Network Analysis of Decision-Making About Recruiting a Living Donor for Kidney Transplantation.

Kidney medicine·2025
Same author

Using Machine Learning to Predict Treatment Outcome in a Concatenated Dataset of Youth Anxiety Treatments.

Child psychiatry and human development·2025
Same author

Leveraging multi-modal data for early prediction of severity in forced transmission outages with hierarchical spatiotemporal multiplex networks.

PloS one·2025

Related Experiment Video

Updated: May 20, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Intrinsic disorder in putative protein sequences.

Uros Midic1, Zoran Obradovic

  • 1Fels Institute for Cancer Research & Molecular Biology, Temple University School of Medicine, 3307 N, Broad St, Philadelphia, PA 19140, USA. uros@temple.edu.

Proteome Science
|July 5, 2012
PubMed
Summary
This summary is machine-generated.

Human protein analysis reveals that predicted disorder in putative sequences may be inaccurate. Gene prediction errors can inflate disorder content, suggesting current methods need reconsideration for reliable protein disorder assessment.

More Related Videos

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

Related Experiment Videos

Last Updated: May 20, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

Area of Science:

  • Genomics
  • Proteomics
  • Bioinformatics

Background:

  • Intrinsically disordered proteins (IDPs) and regions (IDRs) are vital for biological functions despite lacking stable structures.
  • Advanced sequence-based predictors achieve over 80% accuracy for per-residue disorder prediction.
  • A genome-wide study revealed significant differences in predicted disorder between confirmed and putative human proteins.

Purpose of the Study:

  • To investigate if incorrectly annotated gene regions in putative human proteins cause inflated disorder predictions.
  • To test the hypothesis that gene-finding errors contribute to discrepancies in disorder content estimates.

Main Methods:

  • Trained a predictor to distinguish real protein sequences from synthetic sequences mimicking gene-finding errors.
  • Developed a method to create synthetic peptides from non-coding genomic regions and misaligned coding regions.

Main Results:

  • The developed predictor identified a significant fraction of incorrectly assigned regions in putative human protein sequences.
  • These misannotated regions exhibit higher predicted disorder content than correctly assigned regions.
  • This finding partially explains the observed disorder content discrepancy between confirmed and putative proteins.

Conclusions:

  • Provides the first evidence that current methods for predicting disorder in putative protein sequences may be biased.
  • Recommends reconsideration of disorder content estimation practices for putative sequences.
  • Highlights the impact of gene annotation errors on intrinsic disorder predictions.