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

17.8K
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...
17.8K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.7K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.7K
Leaky Scanning02:28

Leaky Scanning

5.1K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.1K
Protein Organization01:24

Protein Organization

6.4K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
6.4K
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.5K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

10.8K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.8K

You might also read

Related Articles

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

Sort by
Same author

Fitness advantage of sequential metabolic strategies emerges from community interactions in strongly fluctuating environments.

PLoS computational biology·2026
Same author

Higher-order interactions in auxotroph communities enhance their resilience to resource fluctuations.

Cell systems·2026
Same author

Unified imputation of missing data modalities and features in multi-omic data via shared representation learning.

bioRxiv : the preprint server for biology·2026
Same author

Intrinsic OASL expression governs heterogeneity in interferon induction during influenza A virus infection.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Single-cell heterogeneity in interferon induction potential is heritable and governed by variation in cell state.

bioRxiv : the preprint server for biology·2025
Same author

Coarse-grained model of serial dilution dynamics in synthetic human gut microbiome.

PLoS computational biology·2025
Same journal

Structure of Perinereis linea erythrocruorin reveals a compact extracellular globin megacomplex.

Structure (London, England : 1993)·2026
Same journal

Meet the author: Stephen Brohawn.

Structure (London, England : 1993)·2026
Same journal

Tetraspanins bring Norrin into focus: Structural insights into ligand-specific Wnt signaling.

Structure (London, England : 1993)·2026
Same journal

Uncovering subtype-selective activation of the K<sub>Ca</sub>3.1 channel by SKA-111.

Structure (London, England : 1993)·2026
Same journal

Identification and structure determination of a type III-Bv CRISPR complex that post-translationally modifies an associated toxin.

Structure (London, England : 1993)·2026
Same journal

Cryo-EM structure of the Arabidopsisthaliana ribosome in translating and non-translating states.

Structure (London, England : 1993)·2026
See all related articles

Related Experiment Video

Updated: Jun 27, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

1.8K

DR-BERT: A protein language model to annotate disordered regions.

Ananthan Nambiar1, John Malcolm Forsyth2, Simon Liu2

  • 1Department of Bioengineering, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA; Carl R. Woese Institute for Genomic Biology, Urbana, IL 61801, USA.

Structure (London, England : 1993)
|May 3, 2024
PubMed
Summary
This summary is machine-generated.

We developed DR-BERT, a novel protein language model for accurately predicting intrinsically disordered regions (IDRs). DR-BERT outperforms existing methods by leveraging contextual information learned during pretraining.

Keywords:
IDPIDRdeep learningdisordermachine learningprotein language modelprotein structure prediction

More Related Videos

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

7.3K
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

68.7K

Related Experiment Videos

Last Updated: Jun 27, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

1.8K
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

7.3K
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

68.7K

Area of Science:

  • Computational biology
  • Protein bioinformatics
  • Machine learning in genomics

Background:

  • Intrinsically disordered regions (IDRs) lack rigid structures but are crucial for protein functions like mediating interactions.
  • Accurate computational annotation of IDRs is essential for understanding cellular mechanisms.

Purpose of the Study:

  • To introduce DR-BERT, a compact protein language model for accurate IDR prediction.
  • To evaluate DR-BERT's performance against existing methods using benchmark datasets.

Main Methods:

  • DR-BERT was pretrained on unannotated proteins.
  • The model was trained to predict IDRs without explicit evolutionary or biophysical data.
  • Performance was assessed on the Critical Assessment of protein Intrinsic Disorder (CAID) and CAID 2 datasets.

Main Results:

  • DR-BERT demonstrated significant improvements over existing IDR prediction tools on the CAID dataset.
  • The model outperformed competitors on two out of four test cases in the CAID 2 dataset.
  • DR-BERT maintained competitiveness on the remaining CAID 2 test cases.

Conclusions:

  • DR-BERT's performance stems from information learned during pretraining and its capacity for contextual information utilization.
  • The model offers a highly accurate and efficient approach for IDR annotation.