Folding Proteins One Loop at a Time

One Loop at a Time

Classic techniques for proving termination require the identification of a measure mapping program states to the elements of a well founded domain and to show that this measure decreases with each iteration of a loop in the program. This is a global termination condition — there is a single measure which must be shown to decrease over all of the loops in the program. In this abstract we look at...

Proving Termination One Loop at a Time

Osmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization

It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...

Osmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization

It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...

AdS4/CFT3 at One Loop

I consider semi-classical type IIA strings rotating in the AdS4 part of AdS4 × CP . The one loop sigma model corrections to this classical solution are used to compute the energy shift, and the result is found to be E − S = f(λ) lnS with f(λ) = √ 2λ− 5 ln 2 2π +O (