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Repulsive interparticle interactions in a denatured protein solution revealed by small angle neutron scattering
V Receveur1, D Durand, M Desmadril
1Laboratoire Léon Brillouin, C.E.A. de Saclay, Gif-sur-Yvette, France. receveur@bioch.ox.ac.uk
FEBS Letters
|May 23, 1998
Summary
Protein unfolding drastically alters intermolecular interactions, revealing denatured polypeptide chains behave as excluded volume polymers. This impacts biological processes and solution non-ideality.
Area of Science:
- Biophysics
- Protein Chemistry
- Polymer Physics
Background:
- Concentration significantly influences biological processes like protein folding.
- Understanding intermolecular interactions is crucial for protein behavior in solution.
- The second virial coefficient quantifies solution non-ideality.
Purpose of the Study:
- To investigate the effect of protein concentration on biological processes.
- To determine the second virial coefficient and radius of gyration of native and denatured phosphoglycerate kinase.
- To elucidate the role of intermolecular interactions in protein unfolding.
Main Methods:
- Small angle neutron scattering (SANS) measurements.
- Determination of the second virial coefficient (A2).
- Measurement of the radius of gyration (Rg) at zero concentration.
Main Results:
- SANS measurements provided A2 for native and denatured phosphoglycerate kinase.
- The unfolding of phosphoglycerate kinase caused a significant change in repulsive intermolecular interactions.
- Rg at zero concentration was determined for both states.
Conclusions:
- Protein unfolding leads to a dramatic alteration in repulsive intermolecular forces.
- These interactions are primarily attributed to the excluded volume behavior of the denatured polypeptide chain.
- The findings provide insights into the physical chemistry of protein denaturation and polymer behavior.