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Energy propagation along polypeptide alpha-helix: experimental data and ab initio zone structure

2019-11Journal article Restricted access
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dc.contributor.authorKhmelinskii, Igor
dc.contributor.authorMakarov, Vladimir, I
dc.date.accessioned2020-07-24T10:51:05Z
dc.date.available2020-07-24T10:51:05Z
dc.date.issued2019-11
dc.description.abstractWe report new theoretical and experimental results that may significantly change our ideas on the workings of life. We performed ab initio analysis of the band structure of periodic α-helix polypeptides (PP) in function of the chain length. Three different calculation approaches were tested: (a) PP described semiempirically as a onedimensional object, with the amino acids substituted by effective atoms; (b) density functional theory (DFT) as implemented in WIEN2k approach, and (c) CRYSTAL-17 software package. The approach (c) was used for the detailed ab initio analysis, as it provided better accuracy in less computation time. We found that the bandgap was weakly dependent on the PP composition, with the asymptotic values in the 0.43 – 0.63 eV range. We estimated the effective electron and hole masses, their mean free path and mobility for the glycine-PP. The electron mobility in the PP conductive band was about half of that in polycrystalline silicon. The PP zone structure was used to study the mechanism of energy transfer along the PP. The current-voltage (I/V) characteristics of Müller cell (MC) intermediate filaments (IFs) from porcine retina were experimentally measured. The measured I/V characteristics show that the IFs behave as semiconductors. These results were discussed in light of the presently reported PP zone structure theory. The results obtained may open new areas in biomedical research and applications.
dc.description.sponsorshipInstitute for Functional Nanomaterials (NSF) [1002410]
dc.description.sponsorshipPR NASA EPSCoR (NASA)National Aeronautics & Space Administration (NASA) [NNX15AK43A]
dc.description.versioninfo:eu-repo/semantics/publishedVersion
dc.identifier.doi10.1016/j.biosystems.2019.104016
dc.identifier.issn0303-2647
dc.identifier.urihttp://hdl.handle.net/10400.1/14195
dc.language.isoeng
dc.peerreviewedyes
dc.publisherElsevier
dc.subjectIntermediate-filaments
dc.subjectProtein structures
dc.subjectMuller cells
dc.subjectModel
dc.subjectQuantum
dc.subjectSelectivity
dc.subjectGeneration
dc.subjectDynamics
dc.subjectSolitons
dc.subjectDensity
dc.subjectPolypeptide α-helix
dc.subjectZone structure analysis
dc.subjectab initio calculations
dc.subjectEnergy propagation mechanism
dc.subjectElectron mobility
dc.subjectEffective electron mass
dc.titleEnergy propagation along polypeptide alpha-helix: experimental data and ab initio zone structure
dc.typejournal article
dspace.entity.typePublication
oaire.citation.startPageUNSP 104016
oaire.citation.titleBioSystems
oaire.citation.volume185
person.familyNameKhmelinskii
person.givenNameIgor
person.identifier0000000420541031
person.identifier.ciencia-id0D1A-CB6C-6316
person.identifier.orcid0000-0002-6116-184X
person.identifier.ridC-9587-2011
person.identifier.scopus-author-id6701444934
rcaap.rightsrestrictedAccess
rcaap.typearticle
relation.isAuthorOfPublicationfcb9f09f-2e99-41fb-8c08-7e1acbc65076
relation.isAuthorOfPublication.latestForDiscoveryfcb9f09f-2e99-41fb-8c08-7e1acbc65076

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