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dc.creatorBreberina, Luka
dc.creatorZlatović, Mario
dc.creatorNikolić, Milan
dc.creatorStojanović, Srđan
dc.date.accessioned2019-12-15T09:46:06Z
dc.date.available2019-12-15T09:46:06Z
dc.date.issued2019
dc.identifier.issn1868-1743
dc.identifier.issn1868-1751
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/3233
dc.description.abstractProtein‐protein interactions are an important phenomenon in biological processes and functions. We used the manually curated non‐redundant dataset of 118 phycocyanin interfaces to gain additional insight into this phenomenon using a robust inter‐atomic non‐covalent interaction analyzing tool PPCheck. Our observations indicate that there is a relatively high composition of hydrophobic residues at the interfaces. Most of the interface residues are clustered at the middle of the range which we call “standard‐size” interfaces. Furthermore, the multiple interaction patterns founded in the present study indicate that more than half of the residues involved in these interactions participate in multiple and water‐bridged hydrogen bonds. Thus, hydrogen bonds contribute maximally towards the stability of protein‐protein complexes. The analysis shows that hydrogen bond energies contribute to about 88 % to the total energy and it also increases with interface size. Van der Waals (vdW) energy contributes to 9.3 %±1.7 % on average in these complexes. Moreover, there is about 1.9 %±1.5 % contribution by electrostatic energy. Nevertheless, the role by vdW and electrostatic energy could not be ignored in interface binding. Results show that the total binding energy is more for large phycocyanin interfaces. The normalized energy per residue was less than −16 kJ mol−1, while most of them have energy in the range from −6 to −14 kJ mol−1. The non‐covalent interacting residues in these proteins were found to be highly conserved. Obtained results might contribute to the understanding of structural stability of this class of evolutionary essential proteins with increased practical application and future designs of novel protein‐bioactive compound interactions.
dc.publisherWileyen
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172001/RS//en
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172035/RS//en
dc.rightsrestrictedAccess
dc.sourceMolecular Informaticsen
dc.subjectPhycocyanins
dc.subjectInterface
dc.subjectHydrogen bonds
dc.subjectHydrophobic interactions
dc.subjectSalt bridges
dc.titleComputational Analysis of Non‐covalent Interactions in Phycocyanin Subunit Interfacesen
dc.typearticleen
dc.rights.licenseARR
dcterms.abstractЗлатовић, Марио; Николић, Милан; Стојановић, Срђан; Бреберина, Лука;
dc.rights.holderWiley
dc.citation.volume38
dc.citation.issue11-12
dc.citation.spage1800145
dc.citation.rankM21~
dc.identifier.doi10.1002/minf.201800145
dc.identifier.scopus2-s2.0-85073932130
dc.type.versionpublishedVersion


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