Unfolding designable structures

Details Unfolding designable structures Unfolding designable structures

2005-10-14

arxiv.org/abs/cond-mat/0510393v2

Physics

Condensed Matter

Soft Condensed Matter

10 pages, 4 figures, Proceeding of the 3rd International Conference NEXT-SigmaPhi

Scientific paper

10.1140/epjb/e2006-00036-x

Among an infinite number of possible folds, nature has chosen only about 1000 distinct folds to form protein structures. Theoretical studies suggest that selected folds are intrinsically more designable than others; these selected folds are unusually stable, a property called the designability principle. In this paper we use the 2D hydrophobic-polar lattice model to classify structures according to their designability, and Langevin dynamics to account for their time evolution. We demonstrate that, among all possible folds, the more designable ones are easier to unfold due to their large number of surface-core bonds.

Affiliated with

Also associated with

No associations

Rating

Unfolding designable structures 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 Unfolding designable structures, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Unfolding designable structures will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-223344