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 Experiment Videos

The interplay between structure and function in intrinsically unstructured proteins.

Peter Tompa1

  • 1Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P.O. Box 7, H-1518 Budapest, Hungary. tompa@enzim.hu

FEBS Letters
|June 10, 2005
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Toward a unified framework for determining conformational ensembles of disordered proteins.

Nature methods·2026
Same author

Expression, purification, and biophysical characterization of liquid-liquid phase separation of full-length hnRNPA2B1.

Protein expression and purification·2025
Same author

DisProt in 2026: enhancing intrinsically disordered proteins accessibility, deposition, and annotation.

Nucleic acids research·2025
Same author

Phase-separating fusion proteins drive cancer by upsetting transcription regulation.

Genome biology·2025
Same author

PPARγ acetylation governs mammary adenocarcinoma tumor growth via acetylated residues that determine DNA sequence-specific binding.

Oncogene·2025
Same author

Targeting protein disorder: the next hurdle in drug discovery.

Nature reviews. Drug discovery·2025
Same journal

Overlapping gut microbiome signatures in aging and disease are characterized by enrichment of medication-associated oral microbes in the gut.

FEBS letters·2026
Same journal

Csk binding to integrin β3 is regulated by tyrosine and threonine phosphorylation of β3.

FEBS letters·2026
Same journal

Mixed-class J-domain protein scaffolds promote expanded aggregate handling and multivalent Hsp70 engagement during functional disaggregase assembly.

FEBS letters·2026
Same journal

Design and analysis strategies for robust microbiome ageing research.

FEBS letters·2026
Same journal

Reconstructing enzyme evolution by protein engineering.

FEBS letters·2026
Same journal

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates.

FEBS letters·2026
See all related articles

Intrinsically unstructured proteins (IUPs) lack a defined structure, challenging traditional protein concepts. Research highlights their in vivo disorder, residual structures, and functional advantages, revealing protein disorder as a mature field.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Intrinsically unstructured proteins (IUPs) are prevalent in proteomes.
  • They possess a unique niche where function is intrinsically linked to structural disorder.
  • Evidence supports their existence without a well-defined folded structure in vitro.

Purpose of the Study:

  • To review novel advances in the field of intrinsically unstructured proteins (IUPs).
  • To examine the in vivo unfolded character of IUPs.
  • To explore the functional benefits derived from their malleable structural state.

Main Methods:

  • Review of recent scientific literature on intrinsically unstructured proteins.
  • Analysis of evidence for in vivo protein disorder.

Related Experiment Videos

  • Investigation of the interplay between residual structure and protein function.

    • Main Results:

    • Compelling evidence supports the existence of IUPs as a distinct protein class.
    • The study details the in vivo unfolded character of IUPs.
    • The interplay between residual structure and function, and the benefits of malleable structures are discussed.

    Conclusions:

    • The concept of protein disorder has matured rapidly.
    • IUPs challenge and transform basic concepts of protein structure and function.
    • Protein disorder is now a fundamental aspect of understanding protein biology.