| pubmed-article:16977342 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16977342 | lifeskim:mentions | umls-concept:C1305923 | lld:lifeskim |
| pubmed-article:16977342 | lifeskim:mentions | umls-concept:C0009609 | lld:lifeskim |
| pubmed-article:16977342 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16977342 | pubmed:dateCreated | 2007-1-25 | lld:pubmed |
| pubmed-article:16977342 | pubmed:abstractText | A coarse-grained model of polypeptide chains confined in a slit formed by two parallel impenetrable surfaces was studied. The chains were flexible heteropolymers (polypeptides) built of two kinds of united atoms-hydrophobic and hydrophilic. The positions of the united atoms were restricted to the vertices of a [310] lattice. The force field consisted of a rigorous excluded volume, a long-distance potential between a pair of amino-acid residues and a local preference for forming secondary structure (helices). The properties of the chains were studied at a wide range of temperatures from good to bad solvent conditions. Monte-Carlo simulations were carried out using the algorithm based on the chain's local changes of conformation and employing the Replica Exchange technique. The influence of the chain length, the distances between the confining surfaces, the temperature and the force field on the dimension and the structure of chains were studied. It was shown that the presence of the confinement chain complicates the process of the chain collapse to low-temperature structures. For some conditions, one can find a rapid decrease of chain size and a second transition indicated by the rapid decrease of the total energy of the system. | lld:pubmed |
| pubmed-article:16977342 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16977342 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16977342 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16977342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16977342 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16977342 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:16977342 | pubmed:issn | 0948-5023 | lld:pubmed |
| pubmed-article:16977342 | pubmed:author | pubmed-author:SikorskiAndrz... | lld:pubmed |
| pubmed-article:16977342 | pubmed:author | pubmed-author:RomiszowskiPi... | lld:pubmed |
| pubmed-article:16977342 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:16977342 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:16977342 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16977342 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16977342 | pubmed:pagination | 327-33 | lld:pubmed |
| pubmed-article:16977342 | pubmed:meshHeading | pubmed-meshheading:16977342... | lld:pubmed |
| pubmed-article:16977342 | pubmed:meshHeading | pubmed-meshheading:16977342... | lld:pubmed |
| pubmed-article:16977342 | pubmed:meshHeading | pubmed-meshheading:16977342... | lld:pubmed |
| pubmed-article:16977342 | pubmed:meshHeading | pubmed-meshheading:16977342... | lld:pubmed |
| pubmed-article:16977342 | pubmed:meshHeading | pubmed-meshheading:16977342... | lld:pubmed |
| pubmed-article:16977342 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:16977342 | pubmed:articleTitle | Computer simulation of polypeptides in a confinement. | lld:pubmed |
| pubmed-article:16977342 | pubmed:affiliation | Department of Chemistry, University of Warsaw, Pasteura 1, 02-093, Warsaw, Poland. sikorski@chem.uw.edu.pl | lld:pubmed |
| pubmed-article:16977342 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16977342 | lld:pubmed |
