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

Structural evolution during protein denaturation as induced by different methods.

S Chodankar1, V K Aswal, J Kohlbrecher

  • 1Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai-400 085, India.

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|June 4, 2008
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

Additive-Driven Micellar Growth and Morphological Transitions in Tetronic Block Copolymers: Insights from Experimental and Computational Study.

The journal of physical chemistry. B·2026
Same author

Protein-Lipid Interactions in a Three-Component POPC-Cholesterol-Sphingomyelin Modulated Membrane.

The journal of physical chemistry. B·2025
Same author

Structural biology at the National Synchrotron Light Source II.

Journal of synchrotron radiation·2025
Same author

Structural and therapeutic properties of salicylic acid-solubilized Pluronic solutions and hydrogels.

Soft matter·2024
Same author

Studying the structural organization of non-membranous protein hemoglobin in a lipid environment after reconstitution.

International journal of biological macromolecules·2023
Same author

Pluronic Induced Interparticle Attraction and Re-entrant Liquid-Liquid Phase Separation in Charged Silica Nanoparticle Suspensions.

Langmuir : the ACS journal of surfaces and colloids·2023
Same journal

Tension on dsDNA bound to ssDNA-RecA filaments may play an important role in driving efficient and accurate homology recognition and strand exchange.

Physical review. E, Statistical, nonlinear, and soft matter physics·2016
Same journal

Publisher's Note: Amplitude-phase coupling drives chimera states in globally coupled laser networks [Phys. Rev. E 91, 040901(R) (2015)].

Physical review. E, Statistical, nonlinear, and soft matter physics·2016
Same journal

Erratum: Shapes of sedimenting soft elastic capsules in a viscous fluid [Phys. Rev. E 92, 033003 (2015)].

Physical review. E, Statistical, nonlinear, and soft matter physics·2016
Same journal

Erratum: Attenuation of excitation decay rate due to collective effect [Phys. Rev. E 90, 022142 (2014)].

Physical review. E, Statistical, nonlinear, and soft matter physics·2016
Same journal

Publisher's Note: Role of connectivity and fluctuations in the nucleation of calcium waves in cardiac cells [Phys. Rev. E 92, 052715 (2015)].

Physical review. E, Statistical, nonlinear, and soft matter physics·2016
Same journal

Publisher's Note: Lattice Boltzmann approach for complex nonequilibrium flows [Phys. Rev. E 92, 043308 (2015)].

Physical review. E, Statistical, nonlinear, and soft matter physics·2016
See all related articles

Bovine serum albumin (BSA) maintains its structure until 60°C, then aggregates and forms a fractal structure. High pressure does not unfold BSA, but urea and surfactants do, with urea-induced unfolding being reversible.

Area of Science:

  • Protein biophysics
  • Structural biology
  • Materials science

Background:

  • Bovine serum albumin (BSA) is a key protein with a native prolate ellipsoidal structure.
  • Understanding protein conformational changes is crucial for various biological and industrial applications.

Purpose of the Study:

  • To investigate the conformational changes of BSA under varying temperature, pressure, and in the presence of denaturants.
  • To characterize the aggregation and gelation behavior of BSA at elevated temperatures.

Main Methods:

  • Small-angle neutron scattering (SANS) for structural analysis.
  • Dynamic light scattering (DLS) for conformational studies.
  • Perturbation using temperature, pressure, urea, and surfactant.

Related Experiment Videos

Main Results:

  • BSA remains stable up to 60°C; denaturation and aggregation occur above this temperature, leading to fractal structures.
  • BSA shows remarkable resistance to pressure-induced unfolding, even up to 450 MPa.
  • Urea concentrations above 4M induce unfolding to a random coil configuration, which is reversible upon dilution.
  • Surfactants denature BSA by forming micelle-like aggregates, stabilizing the complex at higher temperatures.

Conclusions:

  • BSA exhibits distinct denaturation pathways influenced by temperature, pressure, urea, and surfactants.
  • The fractal structure formation indicates aggregation followed by gelation at elevated temperatures.
  • BSA's stability under pressure contrasts with its susceptibility to urea and surfactant-induced denaturation, highlighting the diverse mechanisms of protein structural changes.