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

Proteins can adopt totally different folded conformations.

G Damaschun1, H Damaschun, K Gast

  • 1Humboldt-Universität zu Berlin, Institut für Biologie, c/o Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Strasse 10, Berlin, PF 740238, D-13092, Germany. gdamasc@mdc-berlin.de

Journal of Molecular Biology
|August 17, 1999
PubMed
Summary

Protein structure is influenced by its environment. Yeast phosphoglycerate kinase (PGK) misfolds into more ordered states, like alpha-helices or amyloid-like fibers, under specific conditions.

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

Flip-angle measurement by magnetization inversion: Calibration of magnetization nutation angle in hyperpolarized (3) He magnetic resonance imaging lung experiments.

Magnetic resonance in medicine·2010
Same author

Redox-sensitivity of the dimerization of occludin.

Cellular and molecular life sciences : CMLS·2009
Same author

On the self-association potential of transmembrane tight junction proteins.

Cellular and molecular life sciences : CMLS·2006
Same author

[Does HRCT-emphysema index represent the entire lung?].

RoFo : Fortschritte auf dem Gebiete der Rontgenstrahlen und der Nuklearmedizin·2005
Same author

Effect of environmental conditions on aggregation and fibril formation of barstar.

European biophysics journal : EBJ·2003
Same author

Assembly of amyloid protofibrils via critical oligomers--a novel pathway of amyloid formation.

Journal of molecular biology·2002

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Folding

Background:

  • Protein three-dimensional structure is crucial for function.
  • Environmental interactions significantly impact protein conformation.
  • Yeast phosphoglycerate kinase (PGK) serves as a model system.

Purpose of the Study:

  • To investigate the influence of environmental factors on protein structure.
  • To characterize the non-natively folded states of PGK.
  • To understand the role of acid-unfolded states in protein misfolding.

Main Methods:

  • Analysis of protein secondary structure (alpha-helices, beta-sheets).
  • Induction of protein unfolding using acidic pH and low ionic strength.
  • Induction of misfolding using trifluoroethanol and anions (chloride, trichloroacetate).

Related Experiment Videos

  • Characterization of protein conformation and fiber formation.
  • Main Results:

    • Acidic pH and low ionic strength induce random-walk structures in PGK.
    • Trifluoroethanol transforms acid-unfolded PGK into a flexible alpha-helix.
    • Anions induce amyloid-like fiber formation with extensive beta-sheet structures.
    • Non-natively folded states exhibit higher secondary structure content than native PGK.
    • Misfolding originates from an expanded, acid-unfolded state.

    Conclusions:

    • Environmental conditions dramatically alter protein structure.
    • PGK can adopt highly ordered, non-native conformations.
    • Acid-unfolded states are key intermediates in PGK misfolding pathways.