Jove
Visualize
Contact Us

Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

1.0K
1.0K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.1K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

11.8K
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...
11.8K

You might also read

Related Articles

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

Sort by
Same author

Bis-Tetrazine Fluorogenic (Silicon)-Rhodamine Dyes for Live-Cell Labeling.

Journal of the American Chemical Society·2026
Same author

Direct RNA sequencing enables improved transcriptome assessment and tracking of RNA modifications for medical applications.

Nucleic acids research·2025
Same author

Differential conformational expansion of NUP98-HOXA9 oncoprotein from nanosized assemblies to macrophases.

Nature communications·2025
Same author

Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.

Nature communications·2025
Same author

Promiscuous and multivalent interactions between Eps15 and partner protein Dab2 generate a complex interaction network.

Nature communications·2025
Same author

Current practices in the study of biomolecular condensates: a community comment.

Nature communications·2025
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 Video

Updated: Apr 28, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

16.2K

Mapping multivalency and differential affinities within large intrinsically disordered protein complexes with

Sigrid Milles1, Edward A Lemke

  • 1Structural and Computational Biology Unit, EMBL, Meyerhofstrasse 1, 69117 Heidelberg (Germany).

Angewandte Chemie (International Ed. in English)
|June 6, 2014
PubMed
Summary

Intrinsically disordered proteins (IDPs) bind multiple partners via complex interactions. A new spectroscopy method reveals region-specific binding of nucleoporin153 (Nup153) to nuclear transport receptors (NTRs), clarifying nucleocytoplasmic transport.

Keywords:
FG-nucleoporinfluorescenceintrinsically disordered proteinsligand bindingmultivalency

More Related Videos

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

15.8K
Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

14.5K

Related Experiment Videos

Last Updated: Apr 28, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

16.2K
Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

15.8K
Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

14.5K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Intrinsically disordered proteins (IDPs) exhibit dynamic structures and bind multiple partners.
  • Studying IDP interactions is challenging due to cooperative effects within multiple binding regions.
  • Nucleocytoplasmic transport relies on interactions between IDPs like nucleoporin153 (Nup153) and nuclear transport receptors (NTRs).

Purpose of the Study:

  • To develop and apply a novel spectroscopic method for studying IDP-NTR binding.
  • To characterize the region-specific binding properties of Nup153 to diverse NTRs.
  • To elucidate the implications of these binding properties for nucleocytoplasmic transport.

Main Methods:

  • Combined fluorescence correlation and time-resolved polarization spectroscopy.
  • Detection of segmental backbone mobility within IDP-NTR complexes.
  • Quantitative analysis of binding affinities to distinct Nup153 regions.

Main Results:

  • The developed spectroscopy approach successfully detected local binding properties of Nup153 within unperturbed complexes.
  • Binding affinities of various NTRs to specific Nup153 regions varied significantly, by orders of magnitude.
  • Region-specific binding data were obtained for Nup153, overcoming challenges of studying whole IDPs.

Conclusions:

  • The study presents a powerful method for dissecting IDP interactions.
  • Nup153 exhibits diverse binding affinities to different NTRs across its distinct regions.
  • These findings provide insights into the molecular mechanisms governing the diversity of nucleocytoplasmic transport routes.