Journal
JOURNAL OF COMPUTATIONAL BIOLOGY
Volume 12, Issue 10, Pages 1328-1345Publisher
MARY ANN LIEBERT, INC
DOI: 10.1089/cmb.2005.12.1328
Keywords
inverse protein folding; HP model; protein stability; protein design
Ask authors/readers for more resources
The inverse protein folding problem is that of designing an amino acid sequence which has a particular native protein fold. This problem arises in drug design where a particular structure is necessary to ensure proper protein-protein interactions. In this paper, we show that in the 2D HP model of Dill it is possible to solve this problem for a broad class of structures. These structures can be used to closely approximate any given structure. One of the most important properties of a good protein (in drug design) is its stability-the aptitude not to fold simultaneously into other structures. We show that for a number of basic structures, our sequences have a unique fold.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available