Exact sequence analysis for three-dimensional hydrophobic-polar lattice proteins
Journal of Chemical Physics, ISSN: 0021-9606, Vol: 122, Issue: 11, Page: 114705
2005
- 24Citations
- 11Captures
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Metrics Details
- Citations24
- Citation Indexes24
- 24
- CrossRef19
- Captures11
- Readers11
- 11
Article Description
We have exactly enumerated all sequences and conformations of hydrophobic-polar (HP) proteins with chains of up to 19 monomers on the simple cubic lattice. For two variants of the HP model, where only two types of monomers are distinguished, we determined and statistically analyzed designing sequences, i.e., sequences that have a nondegenerate ground state. Furthermore we were interested in characteristic thermodynamic properties of HP proteins with designing sequences. In order to be able to perform these exact studies, we applied an efficient enumeration method based on contact sets. © 2005 American Institute of Physics.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33244480262&origin=inward; http://dx.doi.org/10.1063/1.1814941; http://www.ncbi.nlm.nih.gov/pubmed/15836241; https://pubs.aip.org/jcp/article/122/11/114705/930216/Exact-sequence-analysis-for-three-dimensional; http://aip.scitation.org/doi/10.1063/1.1814941; https://aip.scitation.org/doi/10.1063/1.1814941
AIP Publishing
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