Local interactions and protein folding : A model study on the square and triangular lattices
(1998) In Journal of Chemical Physics 108(5). p.22452250 Abstract
We study a simple heteropolymer model containing sequenceindependent local interactions on both square and triangular lattices. Sticking to a twoletter code, we investigate the model for varying strength κ of the local interactions; κ=0 corresponds to the wellknown HP model [K. F. Lau and K. A. Dill, Macromolecules 22, 3986 (1989)]. By exhaustive enumerations for short chains, we obtain all structures which act as a unique and pronounced energy minimum for at least one sequence. We find that the number of such designable structures depends strongly on κ. Also, we find that the number of designable structures can differ widely for the two lattices at a given κ. This is the case, for example, at κ=0, which implies that the HP model... (More)
We study a simple heteropolymer model containing sequenceindependent local interactions on both square and triangular lattices. Sticking to a twoletter code, we investigate the model for varying strength κ of the local interactions; κ=0 corresponds to the wellknown HP model [K. F. Lau and K. A. Dill, Macromolecules 22, 3986 (1989)]. By exhaustive enumerations for short chains, we obtain all structures which act as a unique and pronounced energy minimum for at least one sequence. We find that the number of such designable structures depends strongly on κ. Also, we find that the number of designable structures can differ widely for the two lattices at a given κ. This is the case, for example, at κ=0, which implies that the HP model exhibits different behavior on the two lattices. Our findings clearly show that sequenceindependent local properties of the chains can play an important rote in the formation of unique minimum energy structures.
(Less)
 author
 Irbäck, Anders ^{LU} and Sandelin, Erik ^{LU}
 organization
 publishing date
 19980201
 type
 Contribution to journal
 publication status
 published
 in
 Journal of Chemical Physics
 volume
 108
 issue
 5
 pages
 6 pages
 publisher
 American Institute of Physics
 external identifiers

 scopus:0000553651
 ISSN
 00219606
 DOI
 10.1063/1.475605
 language
 English
 LU publication?
 yes
 id
 6215b4d7b34844d2b4a85144bc953db2
 date added to LUP
 20160817 17:53:37
 date last changed
 20180107 11:23:26
@article{6215b4d7b34844d2b4a85144bc953db2, abstract = {<p>We study a simple heteropolymer model containing sequenceindependent local interactions on both square and triangular lattices. Sticking to a twoletter code, we investigate the model for varying strength κ of the local interactions; κ=0 corresponds to the wellknown HP model [K. F. Lau and K. A. Dill, Macromolecules 22, 3986 (1989)]. By exhaustive enumerations for short chains, we obtain all structures which act as a unique and pronounced energy minimum for at least one sequence. We find that the number of such designable structures depends strongly on κ. Also, we find that the number of designable structures can differ widely for the two lattices at a given κ. This is the case, for example, at κ=0, which implies that the HP model exhibits different behavior on the two lattices. Our findings clearly show that sequenceindependent local properties of the chains can play an important rote in the formation of unique minimum energy structures.</p>}, author = {Irbäck, Anders and Sandelin, Erik}, issn = {00219606}, language = {eng}, month = {02}, number = {5}, pages = {22452250}, publisher = {American Institute of Physics}, series = {Journal of Chemical Physics}, title = {Local interactions and protein folding : A model study on the square and triangular lattices}, url = {http://dx.doi.org/10.1063/1.475605}, volume = {108}, year = {1998}, }