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

Kinetic traps in lysozyme folding

T Kiefhaber1

  • 1Abteilung Biophysikalische Chemie, Universität Basel, Switzerland.

Proceedings of the National Academy of Sciences of the United States of America
|September 26, 1995
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

Splintage in the treatment of sagittal band incompetence and extensor tendon subluxation.

The Journal of hand surgery, European volume·2014
Same author

On the unusual fluorescence properties of xanthone in water.

Physical chemistry chemical physics : PCCP·2006
Same author

Origin of apparent fast and non-exponential kinetics of lysozyme folding measured in pulsed hydrogen exchange experiments.

Journal of molecular biology·2001
Same author

Nonprolyl cis peptide bonds in unfolded proteins cause complex folding kinetics.

Nature structural biology·2001
Same author

Apparent two-state tendamistat folding is a sequential process along a defined route.

Journal of molecular biology·2001
Same author

Denaturant-induced movement of the transition state of protein folding revealed by high-pressure stopped-flow measurements.

Proceedings of the National Academy of Sciences of the United States of America·2000
Same journal

Chemotactic self-organization captures the dynamics of mammalian hair follicle patterning.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Tomographic imaging of superconducting order using particle-hole interference.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Inhibitory potential of autologous neutralizing antibodies sets quantitative limits on the rebound-competent HIV-1 reservoir.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Inferring epidemiological parameters under an infectious phylogeography model with visitor dynamics.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Analytical modeling for suction cup designs for skin-interfaced wearable devices.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Improving cell-free metabolism through direct integration of artificial respiratory chains.

Proceedings of the National Academy of Sciences of the United States of America·2026
See all related articles

Lysozyme refolding occurs on parallel pathways. Most molecules slowly fold via intermediates, while a small fraction folds rapidly, suggesting some intermediates trap proteins, hindering direct folding.

Area of Science:

  • Biochemistry
  • Protein Folding Dynamics

Background:

  • Understanding protein folding is crucial for comprehending biological function and disease.
  • Lysozyme is a model protein frequently studied to elucidate folding mechanisms.

Purpose of the Study:

  • To investigate the folding pathways of hen egg white lysozyme using interrupted refolding experiments.
  • To differentiate between fast and slow folding kinetics and identify the role of folding intermediates.

Main Methods:

  • Utilized interrupted refolding experiments, a technique sensitive to native molecule concentration.
  • This method overcomes limitations of optical techniques by directly monitoring native protein formation.
  • Exploited a high energy barrier between native and intermediate states to analyze folding kinetics.

Related Experiment Videos

Main Results:

  • Lysozyme refolding occurs on parallel kinetic pathways under native conditions.
  • 86% of lysozyme molecules refold via a slow pathway involving populated, partially folded intermediates.
  • 14% of molecules exhibit faster folding, consistent with a two-state folding process without intermediates.

Conclusions:

  • The native state formation for the majority of lysozyme molecules is kinetically retarded.
  • Partially structured intermediates appear to kinetically trap molecules, slowing their transition to the native state.
  • These findings suggest complex, multi-pathway folding mechanisms for lysozyme.