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

Interacting processes in protein coagulation.

P L San Biagio1, V Martorana, A Emanuele

  • 1Progetto Sud European Union and INFM, Genova, Italy.

Proteins
|August 19, 1999
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

Engineering the surface of carbon dots for enhanced photoluminescence and controlled plasmonic interactions.

Nanoscale·2025
Same author

Autoptic aspects in a case of autosomal dominant polycystic kidney disease.

La Clinica terapeutica·2024
Same author

The experimental reconstruction of a complicated case of work accident due to a scraper.

La Clinica terapeutica·2024
Same author

Photoinduced charge separation in functional carbon-silver nanohybrids.

Physical chemistry chemical physics : PCCP·2022
Same author

The management of endoscopic retrograde cholangio- pancreatography-related infections risk: results of an italian survey at regional level.

Annali di igiene : medicina preventiva e di comunita·2022
Same author

Do we trust scientific evidence? A multicentre retrospective analysis of first IVF/ICSI cycles before and after the OPTIMIST trial.

Human reproduction (Oxford, England)·2021
Same journal

Engineered HSP90-MP65 Bivalent Fusion Antigen: A Novel Vaccine Candidate Against Invasive Candidiasis.

Proteins·2026
Same journal

Physics-Based Energy Functions for Computational Protein Design.

Proteins·2026
Same journal

Impact of Stabilizing Osmolytes on the Conformational Dynamics of Human and Rat Islet Amyloid Polypeptides.

Proteins·2026
Same journal

Stabilization of Bone Morphogenetic Protein-2 at Physiological pH: Contrasting Roles of CHAPS and Arginine in Aggregation Inhibition.

Proteins·2026
Same journal

Structural Insights Into the Function of Leishmania major Adenylosuccinate Lyase.

Proteins·2026
Same journal

Generalizing the Gaussian Network Model: Spanning-Tree Thermodynamics Shows Entropy-Driven KRAS Activation.

Proteins·2026
See all related articles

Protein conformational changes, crucial for diseases like Alzheimer's, can be studied using bovine serum albumin. This protein model reveals interacting processes of conformational change, solution demixing, and cross-linking driving low-concentration coagulation.

Area of Science:

  • Biochemistry
  • Biophysics
  • Protein Chemistry

Background:

  • Protein self-association and deposit are implicated in neurodegenerative diseases.
  • Conformational changes in proteins can lead to pathological deposits.
  • Studying model systems provides insights into protein aggregation mechanisms.

Purpose of the Study:

  • To investigate the self-association and conformational changes of bovine serum albumin (BSA).
  • To understand the mechanisms underlying protein coagulation at low concentrations.
  • To identify interacting processes involved in BSA conformational change and coagulation.

Main Methods:

  • Experimental studies on bovine serum albumin solutions.
  • Analysis of protein conformational changes.

Related Experiment Videos

  • Observation of solution demixing and protein cross-linking.

    • Main Results:

    • BSA conformational change towards a coagulable form occurs simultaneously with mesoscopic solution demixing.
    • Protein cross-linking is an interacting process in BSA coagulation.
    • These interacting processes facilitate coagulation even at very low protein concentrations.

    Conclusions:

    • The coagulation pathway involving interacting conformational change, demixing, and cross-linking is demonstrated in BSA.
    • This multi-process pathway may be a common feature in polymer coagulation and gelation.
    • BSA serves as a valuable model system for understanding protein self-association and related pathologies.