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...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Protein Organization01:13

Protein Organization

Overview

You might also read

Related Articles

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

Sort by
Same author

Insights into the catalytic mechanism of formate dehydrogenases from different microbial sources.

The FEBS journal·2026
Same author

Sugar-Based Polyesters: From Glux-Diol Synthesis to Its Enzymatic Polymerization.

ACS omega·2026
Same author

Acteoside exerts neuroprotective effects by preventing α-synuclein aggregation and oxidative stress in models of Parkinson's disease.

Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics·2025
Same author

Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1.

Nature communications·2025
Same author

Improving the Proteome-Mining of <i>Schizophyllum commune</i> to Enhance Medicinal Mushroom Applications.

Journal of fungi (Basel, Switzerland)·2025
Same author

Unraveling the molecular grammar and the structural transitions underlying the fibrillation of a viral fibrillogenic domain.

Protein science : a publication of the Protein Society·2025

Related Experiment Video

Updated: May 27, 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

Length-dependent compaction of intrinsically disordered proteins.

Vladimir N Uversky1, Carlo Santambrogio, Stefania Brocca

  • 1Department of Molecular Medicine, College of Medicine, University of South Florida, Tampa, FL 33612, USA.

FEBS Letters
|December 6, 2011
PubMed
Summary

Protein chain length influences compaction, with larger intrinsically disordered proteins (IDPs) adopting more compact states. Sequence features drive group differences, while length modulates compaction within IDP types.

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

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Related Experiment Videos

Last Updated: May 27, 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

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Dynamics

Background:

  • Intrinsically disordered proteins (IDPs) lack stable tertiary structures.
  • IDPs exhibit dynamic conformational ensembles.
  • Understanding IDP compaction is crucial for their function.

Purpose of the Study:

  • To investigate the impact of protein chain length on the compaction of different intrinsically disordered protein types.
  • To compare compaction across native coil (NC), pre-molten globule (PMG), and molten globule (MG) states.
  • To elucidate the interplay between sequence features and chain length in determining IDP compactness.

Main Methods:

  • Utilized a compaction index (CI) normalized for chain length.
  • Analyzed three distinct IDP types: native coil (NC), pre-molten globule (PMG), and molten globule (MG).
  • Quantified the relationship between protein size and structural compactness.

Main Results:

  • Observed significant variability in compactness related to chain length within each IDP group.
  • Demonstrated that larger proteins generally exhibit more compact states.
  • Identified sequence features as primary drivers of differences between IDP groups, with chain length acting as a secondary modulator.

Conclusions:

  • Chain length plays a modulating role in the compaction of intrinsically disordered proteins.
  • The observed compaction patterns support a cooperative mechanism driven by weak interactions in protein collapse.
  • Further research into IDP conformational dynamics and sequence-structure relationships is warranted.