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

Conformational studies on rat alpha-lactalbumin.

K Nitta, S Sugai, R V Prasad

    Biochimica Et Biophysica Acta
    |April 27, 1984
    PubMed
    Summary

    Rat alpha-lactalbumin exhibits unique structural properties due to its extended carboxyl terminus and glycosylation. Its unfolding differs from bovine alpha-lactalbumin, indicating distinct stability and structural mechanisms.

    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

    Glomerular crescents predominantly express cadherin-catenin complex in pauci-immune-type crescentic glomerulonephritis.

    Histopathology·2003
    Same author

    C4d deposition in the glomeruli and peritubular capillaries associated with transplant glomerulopathy.

    Clinical transplantation·2003
    Same author

    Search for nu(e) from the sun at Super-Kamiokande-I.

    Physical review letters·2003
    Same author

    Search for supernova relic neutrinos at Super-Kamiokande.

    Physical review letters·2003
    Same author

    Catheter dysfunction and thrombosis of double-lumen hemodialysis catheters placed in the femoral vein.

    Clinical nephrology·2002
    Same author

    Energetics of three-state unfolding of a protein: canine milk lysozyme.

    Protein engineering·2002

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Protein Chemistry

    Background:

    • Rat alpha-lactalbumin possesses a unique 17-amino-acid carboxyl-terminal extension and a carbohydrate moiety at Asn-45, distinguishing it from other alpha-lactalbumins.
    • The native structure of rat alpha-lactalbumin shares similarities with bovine alpha-lactalbumin.

    Purpose of the Study:

    • To investigate the reversible unfolding of rat alpha-lactalbumin under varying conditions (pH, heat, guanidine hydrochloride).
    • To compare the structural stability and unfolding mechanisms of rat alpha-lactalbumin with those of bovine alpha-lactalbumin.

    Main Methods:

    • Circular dichroism spectroscopy was employed to analyze protein structure changes.
    • Experiments were conducted across a wavelength range of 193-310 nm.
    • Varying pH, temperature, and guanidine hydrochloride concentrations were used to induce unfolding.

    Main Results:

    • Acidification induced a conformational change in rat alpha-lactalbumin, resembling the 'A state' of bovine alpha-lactalbumin.
    • Heat-induced unfolding of the tertiary structure was highly cooperative.
    • Guanidine hydrochloride-induced unfolding did not follow a two-state mechanism, unlike bovine alpha-lactalbumin.
    • Rat alpha-lactalbumin displayed lower stability in secondary and tertiary structures compared to bovine alpha-lactalbumin.

    Conclusions:

    • Rat alpha-lactalbumin exhibits distinct unfolding characteristics compared to bovine alpha-lactalbumin, attributed to its unique structural features.
    • The observed differences in stability and unfolding mechanisms highlight the impact of terminal extensions and glycosylation on protein structure and dynamics.

    Related Experiment Videos