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

Response functions of proteins.

J Rösgen1, H J Hinz

  • 1Institut für Physikalische Chemie, Westfälische Wilhelms-Universität, Münster, Germany.

Biophysical Chemistry
|January 13, 2000
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

The 'Janus' nature of proteins: systems at the verge of the microscopic and macroscopic world.

Biophysical chemistry·2006
Same author

Partial molar volumes of proteins: amino acid side-chain contributions derived from the partial molar volumes of some tripeptides over the temperature range 10-90 degrees C.

Biophysical chemistry·2006
Same author

Protein heat capacity: inconsistencies in the current view of cold denaturation.

Biophysical chemistry·2006
Same author

Pressure-modulated differential scanning calorimetry. An approach to the continuous, simultaneous determination of heat capacities and expansion coefficients.

Analytical chemistry·2006
Same author

Matrix-assisted in vitro refolding of Pseudomonas aeruginosa class II polyhydroxyalkanoate synthase from inclusion bodies produced in recombinant Escherichia coli.

The Biochemical journal·2001
Same author

Folding energetics of ligand binding proteins. I. Theoretical model.

Journal of molecular biology·2001

This study presents analytical solutions for determining protein response functions, combining heat capacity, expansion coefficient, and compressibility measurements. This approach maximizes thermodynamic insights into protein folding and dynamics.

Area of Science:

  • Biophysics
  • Thermodynamics
  • Protein Science

Background:

  • Protein folding thermodynamics are crucial for understanding protein behavior.
  • Multiple techniques like calorimetry and densimetry offer insights into protein dynamics.
  • Combining different response functions provides a more comprehensive thermodynamic description.

Purpose of the Study:

  • To develop analytical solutions for determining key thermodynamic response functions.
  • To demonstrate how to extract maximum thermodynamic information from experimental measurements.
  • To advance the comprehensive thermodynamic description of protein behavior.

Main Methods:

  • Utilizing differential scanning calorimetry (Cp) to measure heat capacity.
  • Employing differential scanning densimetry (αp) to determine expansion coefficient.

Related Experiment Videos

  • Applying sound velocity measurements (κT) for compressibility analysis.
  • Main Results:

    • Analytical solutions were derived for calculating response functions (Cp, αp, κT).
    • Demonstrated methods for maximizing thermodynamic data extraction from measurements.
    • Established a framework for integrating diverse thermodynamic data.

    Conclusions:

    • Combining heat capacity, expansion coefficient, and compressibility measurements offers a powerful approach.
    • The derived analytical solutions facilitate a deeper understanding of protein thermodynamics.
    • This integrated method enhances the characterization of protein dynamics and folding.