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dc.creatorBorozan, Sunčica
dc.creatorStojanović, Srđan
dc.date.accessioned2019-01-30T17:35:23Z
dc.date.available2019-01-30T17:35:23Z
dc.date.issued2013
dc.identifier.issn1476-9271
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/1235
dc.description.abstractIn this work, we have analyzed the influence of halogen bonding to the stability of 44 complexes of proteins and non-natural amino acids. Fluorine- and chlorine-containing non-natural amino acids are more prevalent in the dataset, and an even larger number of contacts made by iodine-containing ligands are found. Only few halogen bonds with the hydroxyl oxygens and carboxylate side chains are found in the dataset. Halogen bonds with the nitrogen-containing side chains have higher occurrence than other acceptors. Backbone carbonyl oxygens and nitrogens are to a substantial extent involved in our dataset We have observed a small percentage of interactions involving water as hydrogen bond donors. Additionally, most of the interacting residues comprising the interfaces also show a great degree of conservation. There is a clear interaction hot spot at distances of 3.5-3.7 angstrom and Theta(1) angles of 100-120 degrees. There is also a cluster of contacts featuring short distances (2.6-2.9 angstrom) but only nearly optimal Theta(1) angles (140-160 degrees). 51.3% of stabilizing residues are involved in building halogen bonds with the non-natural amino acids. We discovered three types of structural motifs significantly over-represented: beta-turn-ir, beta-turn-il and niche-4r. The halogen-bonding statistics of the dataset do not show any preference for alpha-helices (36%), beta-sheets (36%), or turns/coils (28%) structures. Most of the amino acid residues that were involved in halogen bonds prefer to be in the solvent excluded environment (buried). Furthermore, we have shown that in amino acid-protein complexes halogen atoms can sometimes be involved in hydrogen bonding interactions with hydrogen bonding-donors. The results from this study might be used for the rational design of halogenated ligands as inhibitors and drugs, and in biomolecular engineering.en
dc.publisherElsevier Sci Ltd, Oxford
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172001/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/173034/RS//
dc.rightsrestrictedAccess
dc.sourceComputational Biology and Chemistry
dc.subjectHalogen bondingen
dc.subjectProteinsen
dc.subjectNon-natural amino acidsen
dc.subjectComplexesen
dc.subjectStabilization centersen
dc.titleHalogen bonding in complexes of proteins and non-natural amino acidsen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractБорозан, Сунцица З.; Стојановић, Срђан;
dc.citation.volume47
dc.citation.spage231
dc.citation.epage239
dc.citation.other47: 231-239
dc.citation.rankM22
dc.identifier.pmid24200696
dc.identifier.doi10.1016/j.compbiolchem.2013.10.002
dc.identifier.rcubConv_3092
dc.identifier.scopus2-s2.0-84887443028
dc.identifier.wos000329270700029
dc.type.versionpublishedVersion


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