Understanding the determinants of stability and folding of small globular proteins from their energetics

Details Understanding the determinants of stability and folding of small globular proteins from their energetics Understanding the determinants of stability and folding of small globular proteins from their energetics

2003-01-30

arxiv.org/abs/cond-mat/0301582v1

Physics

Condensed Matter

Soft Condensed Matter

Scientific paper

The results of minimal model calculations suggest that the stability and the kinetic accessibility of the native state of small globular proteins are controlled by few "hot" sites. By mean of molecular dynamics simulations around the native conformation, which simulate the protein and the surrounding solvent at full--atom level, we generate an energetic map of the equilibrium state of the protein and simplify it with an Eigenvalue decomposition. The components of the Eigenvector associated with the lowest Eigenvalue indicate which are the "hot" sites responsible for the stability and for the fast folding of the protein. Comparison of these predictions with the results of mutatgenesis experiments, performed for five small proteins, provide an excellent agreement.

Affiliated with

Also associated with

No associations

Rating

Understanding the determinants of stability and folding of small globular proteins from their energetics 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 Understanding the determinants of stability and folding of small globular proteins from their energetics, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Understanding the determinants of stability and folding of small globular proteins from their energetics will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-335656