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

Protein Folding01:22

Protein Folding

Overview
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
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

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.
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...

You might also read

Related Articles

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

Sort by
Same author

Tuning Connectivity in Hybrid Organic-Inorganic Antimony Halides through Reactant Concentration Effects.

Inorganic chemistry·2026
Same author

Machiavellianism, level of personality functioning, and maladaptive personality traits: mediation analyses in a clinical sample.

Frontiers in psychiatry·2026
Same author

Amide isomerization pathways II: Tracing geometrical prerequisites of acid-catalyzed amide cis-trans isomerization in globular proteins.

The Journal of chemical physics·2026
Same author

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation.

The FEBS journal·2026
Same author

Screening for Personality Disorders Using the Level of Personality Functioning: Diagnostic Accuracy of the LPFS-BF 2.0 in Clinical and <i>Sine Morbo</i> Samples.

Journal of personality disorders·2026
Same author

Improving Protein Structure Determination by Integrating Ensemble-Driven Molecular Dynamics with Chemical Shift-Based Restraints.

Journal of chemical information and modeling·2026

Related Experiment Video

Updated: May 15, 2026

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

Structural insights into the Trp-cage folding intermediate formation.

Petra Rovó1, Pál Stráner, András Láng

  • 1Laboratory of Structural Chemistry and Biology, Institute of Chemistry and Protein Modeling Group of HAS-ELTE, Eötvös Loránd University, 1117 Budapest, Pázmány Péter sétány 1/A, Hungary.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|January 16, 2013
PubMed
Summary

The smallest protein, Trp-cage, exhibits multistate folding with distinct intermediates detected using NMR. This study reveals the atomic details of its folding pathways and intermediate structures.

More Related Videos

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
08:27

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

Related Experiment Videos

Last Updated: May 15, 2026

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
08:27

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

Area of Science:

  • Biochemistry and Molecular Biophysics
  • Protein Folding Dynamics
  • Structural Biology

Background:

  • The Trp-cage is the smallest known protein, making it a model system for studying protein folding.
  • Understanding protein folding pathways is crucial for deciphering biological function and disease mechanisms.

Purpose of the Study:

  • To elucidate the multistate folding scenario of the Trp-cage miniprotein in atomic detail.
  • To characterize intermediate states during folding and unfolding processes.
  • To provide experimental data for validating computational simulations of protein folding.

Main Methods:

  • Temperature-dependent Nuclear Magnetic Resonance (NMR) spectroscopy on isotopically labeled Trp-cage.
  • Development of a deconvolution technique for analyzing fast-exchanging states.
  • Nonlinear fitting methods to determine thermodynamic parameters and chemical shifts.
  • Heteronuclear relaxation studies and Molecular Dynamics (MD) simulations.

Main Results:

  • Detection and characterization of distinct intermediate states at neutral and acidic pH.
  • Identification of a native-like intermediate at neutral pH and a dynamic intermediate pair at acidic pH.
  • Characterization of the G(11)-G(15) α-helix in the native-like intermediate and cis/trans isomerism of the G(11)-P(12) bond in acidic intermediates.
  • Elucidation of backbone mobility and structural rearrangements through relaxation studies and MD simulations.

Conclusions:

  • The Trp-cage exhibits a complex multistate folding pathway with pH-dependent intermediates.
  • Experimental data provides atomic-level insights into protein folding energy landscapes.
  • The findings offer a valuable benchmark for computational protein folding simulations.