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

Folding versus aggregation: polypeptide conformations on competing pathways.

Thomas R Jahn1, Sheena E Radford

  • 1Astbury Centre for Structural and Molecular Biology, Institute of Molecular and Cellular Biology, University of Leeds, Mount Preston Street, Leeds LS2 9JT, UK.

Archives of Biochemistry and Biophysics
|June 26, 2007
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

Author Correction: High-throughput discovery of fluoroprobes that recognize amyloid fibril polymorphs.

Nature chemistry·2026
Same author

Nanopipettes Enable Native Mass Spectrometry Studies of the Intrinsically Disordered Protein α-Synuclein in Biochemical Buffers.

Analytical chemistry·2026
Same author

Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.

Chemical reviews·2026
Same author

Checking in on proteostasis.

Nature structural & molecular biology·2026
Same author

Amyloid fibril polymorphism: Structural mechanisms of assembly and the links to disease.

Current opinion in structural biology·2026
Same author

In silico peptide self-assembly reveals the importance of N-terminal motifs and the inhibition mechanism of the mutation L38M in α-synuclein fibrillation.

Protein science : a publication of the Protein Society·2026
Same journal

Cortical Cholesterol Deficit and Reduced Network Excitability in ApoE-Deficient Mice.

Archives of biochemistry and biophysics·2026
Same journal

Unraveling zinc's impact: Variable effects across concentrations in Phaseolus coccineus thylakoids.

Archives of biochemistry and biophysics·2026
Same journal

Characterizing tumor-associated endothelial cells in clear cell renal cell carcinoma via scRNA-seq and Bulk RNA-seq: construction of a prognostic risk signature.

Archives of biochemistry and biophysics·2026
Same journal

FOSB-Histone deacetylase 6 axis drives hepcidin-mediated ferroptosis in pulmonary ischemia-reperfusion injury.

Archives of biochemistry and biophysics·2026
Same journal

Sevoflurane preconditioning alleviates hypoxia-reoxygenation-induced myocardial injury via regulating the MIR210HG/miR-377-3p/PUM2 axis.

Archives of biochemistry and biophysics·2026
Same journal

Structural and kinetic analysis of human NQO1: Evidence for therapeutic inhibition by racemic warfarin.

Archives of biochemistry and biophysics·2026
See all related articles

Protein aggregation is a key factor in protein energy landscapes and disease. Understanding misfolded protein states and aggregation pathways is crucial for developing new therapeutic strategies.

Area of Science:

  • Biochemistry
  • Biophysics
  • Structural Biology

Background:

  • Protein aggregation is implicated in numerous human diseases.
  • Understanding the mechanisms of protein misfolding and aggregation is critical.
  • Protein energy landscapes govern folding and aggregation pathways.

Purpose of the Study:

  • To review recent experimental and theoretical advances in understanding protein aggregation.
  • To elucidate the conformational properties of protein ensembles involved in aggregation.
  • To discuss the interplay between protein folding and aggregation pathways.

Main Methods:

  • Utilizing established experimental techniques for protein folding analysis.
  • Employing computational approaches to study aggregation mechanisms.

Related Experiment Videos

  • Integrating biochemical, biophysical, and cell-biological experimental data.

    • Main Results:

    • Detailed insights into the conformational properties of dynamic protein ensembles.
    • Elucidation of pathways leading to amyloid fibrils and related aggregates.
    • Understanding the partitioning of non-native species between folding and aggregation.

    Conclusions:

    • Synergistic experimental approaches provide detailed insights into protein aggregation.
    • Complex protein energy landscapes dictate aggregation propensity.
    • Further research is needed to fully understand and target protein aggregation in disease.