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

Thermodynamic study of the apomyoglobin structure.

Y V Griko1, P L Privalov, S Y Venyaminov

  • 1Institute of Protein Research, Academy of Sciences of the U.S.S.R., Pushchino, Moscow Region.

Journal of Molecular Biology
|July 5, 1988
PubMed
Summary

Sperm whale apomyoglobin exhibits a stable, compact structure near neutral pH, which reversibly denatures upon heating or cooling from 30°C. This protein

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

Thermodynamic basis of the α-helix and DNA duplex.

European biophysics journal : EBJ·2021
Same author

Hydroxycobalamin catalyzes the oxidation of diethyldithiocarbamate and increases its cytotoxicity independently of copper ions.

Redox biology·2018
Same author

[NMR study of human biological fluids for detection of pathologies].

Biomeditsinskaia khimiia·2015
Same author

[NMR studies of water-gas interactions].

Biofizika·2014
Same author

Heat denaturation of ribonuclease.

Biophysical chemistry·2012
Same author

From fragments to morphogenesis: NMR spectroscopy of metabolites in the apex of the roots of onion.

Doklady. Biochemistry and biophysics·2012

Area of Science:

  • Biochemistry
  • Structural Biology
  • Thermodynamics

Background:

  • Apomyoglobin, a key protein, undergoes structural changes influenced by environmental factors.
  • Understanding protein stability is crucial for molecular biology and drug development.

Purpose of the Study:

  • To thermodynamically characterize sperm whale apomyoglobin structure.
  • To investigate the impact of pH and temperature on apomyoglobin stability and denaturation.

Main Methods:

  • Scanning microcalorimetry
  • Viscosimetry
  • Nuclear magnetic resonance (NMR) spectrometry
  • Circular dichroism (CD) spectrometry
  • Electrometric and calorimetric titration

Related Experiment Videos

Main Results:

  • Apomyoglobin displays a compact, unique structure with a hydrophobic core at neutral pH.
  • Maximum protein stability observed around 30°C.
  • Reversible denaturation occurs upon deviation from 30°C, indicating a cooperative transition between native and denatured states.
  • Denatured state compactness and ellipticity are pH-dependent, approaching random coil values below pH 4.0.

Conclusions:

  • Sperm whale apomyoglobin exhibits distinct native and denatured states.
  • Protein structure and stability are significantly modulated by pH and temperature.
  • The study provides insights into the thermodynamic principles governing protein folding and denaturation.