Please use this identifier to cite or link to this item:
https://research.matf.bg.ac.rs/handle/123456789/344
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Malkov, Saša | en_US |
dc.contributor.author | Zivković, Miodrag V | en_US |
dc.contributor.author | Beljanski, Milos V | en_US |
dc.contributor.author | Hall, Michael B | en_US |
dc.contributor.author | Zarić, Snezana D | en_US |
dc.date.accessioned | 2022-08-10T12:10:01Z | - |
dc.date.available | 2022-08-10T12:10:01Z | - |
dc.date.issued | 2008 | - |
dc.identifier.issn | 16102940 | en |
dc.identifier.uri | https://research.matf.bg.ac.rs/handle/123456789/344 | - |
dc.description.abstract | The correlation between the primary and secondary structures of proteins was analysed using a large data set from the Protein Data Bank. Clear preferences of amino acids towards certain secondary structures classify amino acids into four groups: alpha-helix preferrers, strand preferrers, turn and bend preferrers, and His and Cys (the latter two amino acids show no clear preference for any secondary structure). Amino acids in the same group have similar structural characteristics at their Cbeta and Cgamma atoms that predicts their preference for a particular secondary structure. All alpha-helix preferrers have neither polar heteroatoms on Cbeta and Cgamma atoms, nor branching or aromatic group on the Cbeta atom. All strand preferrers have aromatic groups or branching groups on the Cbeta atom. All turn and bend preferrers have a polar heteroatom on the Cbeta or Cgamma atoms or do not have a Cbeta atom at all. These new rules could be helpful in making predictions about non-natural amino acids. | en |
dc.language.iso | en | en |
dc.relation.ispartof | Journal of molecular modeling | en_US |
dc.subject | Amino acid | en |
dc.subject | Protein | en |
dc.subject | Protein secondary structure | en |
dc.subject | Statistical correlation | en |
dc.subject.mesh | Amino Acid Sequence | en |
dc.subject.mesh | Amino Acids | en |
dc.subject.mesh | Computer Simulation | en |
dc.subject.mesh | Models, Chemical | en |
dc.subject.mesh | Protein Structure, Secondary | en |
dc.title | A reexamination of the propensities of amino acids towards a particular secondary structure: classification of amino acids based on their chemical structure | en_US |
dc.type | Article | en_US |
dc.identifier.doi | 10.1007/s00894-008-0313-0 | - |
dc.identifier.pmid | 18504624 | - |
dc.identifier.scopus | 2-s2.0-47249128045 | - |
dc.identifier.url | https://api.elsevier.com/content/abstract/scopus_id/47249128045 | - |
dc.contributor.affiliation | Informatics and Computer Science | en_US |
dc.relation.firstpage | 769 | en_US |
dc.relation.lastpage | 775 | en_US |
dc.relation.volume | 14 | en_US |
dc.relation.issue | 8 | en_US |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | none | - |
item.openairetype | Article | - |
crisitem.author.dept | Informatics and Computer Science | - |
crisitem.author.orcid | 0000-0002-4385-6322 | - |
Appears in Collections: | Research outputs |
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