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

Collapse and cooperativity in protein folding

A D Miranker1, C M Dobson

  • 1New Chemistry Laboratory, Oxford Centre for Molecular Sciences, University of Oxford, UK. miranker@bioch.ox.ac.uk

Current Opinion in Structural Biology
|February 1, 1996
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

Structural Characteristics of α-Synuclein Oligomers.

International review of cell and molecular biology·2017
Same author

Spatial propagation of protein polymerization.

Physical review letters·2014
Same author

The effects of guanidine hydrochloride on the 'random coil' conformations and NMR chemical shifts of the peptide series GGXGG.

Journal of biomolecular NMR·2010
Same author

Amyloidogenicity and aggregate cytotoxicity of human glucagon-like peptide-1 (hGLP-1).

Protein and peptide letters·2009
Same author

Disseminated gonococcal infection in pregnancy.

Journal of obstetrics and gynaecology : the journal of the Institute of Obstetrics and Gynaecology·2009
Same author

Conformations and conformational dynamics of proteins in solution studied by nuclear magnetic double resonance.

Biophysical journal·2009
Same journal

Molecular crowding and amyloidogenic self-assembly: Emergent perspectives from modern computations.

Current opinion in structural biology·2026
Same journal

Recent advances in modeling and simulation of biological phenomena in crowded and cellular environments.

Current opinion in structural biology·2026
Same journal

Progress toward linking single-molecule behavior and condensate material properties.

Current opinion in structural biology·2026
Same journal

Tomogram exploration through template matching and deep learning.

Current opinion in structural biology·2026
Same journal

A comparative review of cryo-electron ptychography: Biological applications and future perspectives.

Current opinion in structural biology·2026
Same journal

Metabolic disruptions through a three-dimensional genomic lens.

Current opinion in structural biology·2026
See all related articles

Protein folding drives molecular compactness and cooperativity, leading to native-like structures. Recent experiments illuminate these protein folding pathways and their associated structural dynamics.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Protein folding is crucial for biological function, involving the acquisition of specific three-dimensional structures.
  • Understanding protein folding pathways is essential for deciphering molecular mechanisms and disease pathologies.

Purpose of the Study:

  • To elucidate the relationship between polypeptide chain folding, structural compactness, and cooperativity.
  • To investigate the role of local and global interactions in achieving native-like protein architecture.
  • To connect experimental observations with theoretical models of protein folding pathways.

Main Methods:

  • Utilizing recent experimental techniques to probe protein structure dynamics.
  • Analyzing data to understand the interplay of local and global forces during folding.

Related Experiment Videos

  • Correlating experimental findings with established protein folding theories.

    • Main Results:

    • Experimental evidence highlights the link between folding, compactness, and cooperative dynamics.
    • Observations confirm the formation of native-like molecular architecture through specific folding pathways.
    • Key insights into the sequence of events governing protein structure formation were gained.

    Conclusions:

    • Protein folding is a complex process involving both local and global cooperativity to achieve functional structures.
    • Recent experimental findings provide a clearer picture of the pathways governing protein folding.
    • This research deepens our understanding of how polypeptide chains attain their native-like molecular architecture.