Physics – Biological Physics
Scientific paper
2002-04-01
Biophys. J. 83, 2801 (2002).
Physics
Biological Physics
Scientific paper
A lattice based model of a protein is used to study the dimerization equilibrium of the GCN4 leucine zipper. Replica exchange Monte Carlo is used to determine the free energy of both the monomeric and dimeric forms as a function of temperature. The method of coincidences is then introduced to explicitly calculate the entropy loss associated with dimerization, and from it the free energy difference between monomer and dimer, as well as the corresponding equilibrium reaction constant. We find that the entropy loss of dimerization is a strong function of energy (or temperature), and that it is much larger than previously estimated, especially for high energy states. The results confirm that it is possible to study the dimerization equilibrium of GCN4 at physiological concentrations within the reduced representation of the protein employed.
Kolinski Andrzej
Skolnick Jeffrey
Vinals Jorge
No associations
LandOfFree
Numerical estimation of entropy loss on dimerization: improved prediction of the quaternary structure of the GCN4 leucine zipper does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.
If you have personal experience with Numerical estimation of entropy loss on dimerization: improved prediction of the quaternary structure of the GCN4 leucine zipper, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Numerical estimation of entropy loss on dimerization: improved prediction of the quaternary structure of the GCN4 leucine zipper will most certainly appreciate the feedback.
Profile ID: LFWR-SCP-O-316789