Gauge field theory of chirally folded homopolymers with applications to folded proteins.
We combine the principle of gauge invariance with extrinsic string geometry to develop a lattice model that can be employed to theoretically describe properties of chiral, unbranched homopolymers. We find that in its low temperature phase the model is in the same universality class with proteins that are deposited in the Protein Data Bank, in the sense of the compactness index. We apply the model to analyze various statistical aspects of folded proteins. Curiously we find that it can produce results that are a very good good match to the data in the Protein Data Bank.
Danielsson
Ulf H
UH
Department of Physics and Astronomy, Uppsala University, Sweden. ulf.danielsson@physics.uu.se
Lundgren
Martin
M
Niemi
Antti J
AJ
D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D011108:Polymers / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*
D011108:Polymers; D011506:Proteins