Use este identificador para citar ou linkar para este item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1093429
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dc.contributor.authorMAZONI, I.
dc.contributor.authorBORRO, L. C.
dc.contributor.authorJARDINE, J. G.
dc.contributor.authorYANO, I. H.
dc.contributor.authorSALIM, J. A.
dc.contributor.authorNESHICH, G.
dc.date.accessioned2018-07-21T01:04:12Z-
dc.date.available2018-07-21T01:04:12Z-
dc.date.created2018-07-20
dc.date.issued2018
dc.identifier.citationPlos One, v. 13, n. 7, p. 1-25, 2018.
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/1093429-
dc.descriptionProtein secondary structure elements (PSSEs) such as [alfa]-helices, [beta]-strands, and turns are the primary building blocks of the tertiary protein structure. Our primary interest here is to reveal the characteristics of the nanoenvironment formed by both PSSEs and their surrounding amino acid residues (AARs), which might contribute to the general understanding of how proteins fold.
dc.language.isoengeng
dc.rightsopenAccesseng
dc.subjectTeste estatístico
dc.subjectEstrutura secundária de proteína
dc.subjectMANOVA
dc.subjectStudent's t-test
dc.subjectKolmogorov-Smirnov test
dc.subjectBlue Star STING
dc.subjectProtein secondary structure elements
dc.subjectAmino acid residues
dc.titleStudy of specific nanoenvironments containing α-helices in all-α and ([α]+[β])+([α]/[β]) proteins.
dc.typeArtigo de periódico
dc.date.updated2018-07-21T01:04:12Zpt_BR
dc.subject.thesagroProteína
dc.subject.thesagroAminoácido
dc.subject.nalthesaurusProteins
dc.subject.nalthesaurusStatistical analysis
dc.subject.nalthesaurusAmino acids
dc.description.notesArtigo e0200018.
riaa.ainfo.id1093429
riaa.ainfo.lastupdate2020-12-30 -02:00:00
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0200018
dc.contributor.institutionIVAN MAZONI, CNPTIA; LUIZ CÉSAR BORRO, IB/Unicamp; JOSE GILBERTO JARDINE, CNPM; INACIO HENRIQUE YANO, CNPTIA; JOSÉ AUGUSTO SALIM, USP; GORAN NESIC, CNPTIA.
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