Please use this identifier to cite or link to this item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/9056
Full metadata record
DC FieldValueLanguage
dc.contributor.authorREIS, F. de C.
dc.contributor.authorCALDAS, L. F.
dc.contributor.authorSANTOS, M. T. dos
dc.contributor.authorFALCÃO, P. R. K.
dc.contributor.authorNESHICH, G.
dc.contributor.authorOTTOBONI, L. M. M.
dc.date.accessioned2022-05-17T19:12:39Z-
dc.date.available2022-05-17T19:12:39Z-
dc.date.created2006-08-29
dc.date.issued2006
dc.identifier.citationIn: ANNUAL INTERNATIONAL CONFERENCE ON INTELLIGENT SYSTEMS FOR MOLECULAR BIOLOGY, 14.; ANNUAL AB3C CONFERENCE, 2., 2006, Fortaleza. Conference Program... Fortaleza: ISCB, 2006.
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/9056-
dc.descriptionShort Abstract: We report the molecular modeling of the polypeptide deformylase from A. ferrooxidans. The model presents all the conserved residues that characterize this family of protein including, the HEXXH domain and the Gln50, Cys90, Leu91, Ser92 residues. Interactions among many residues showed some important differences when compared with the reference structure.
dc.language.isoeng
dc.rightsopenAccess
dc.subjectModelo molecular
dc.subjectModelagem molecular
dc.titleMolecular modeling of polypeptide deformylase from acidithiobacillus ferrooxidans.
dc.typeResumo em anais e proceedings
dc.subject.thesagroBactéria
dc.subject.nalthesaurusAcidithiobacillus ferrooxidans
dc.description.notesISMB, X-MEETING 2006. Poster I-95. Na publicação: Paula K. Falcão.
dc.format.extent2Não paginado.
riaa.ainfo.id9056
riaa.ainfo.lastupdate2022-05-17
dc.contributor.institutionFERNANDA DE CASTRO REIS, CBMEG/Unicamp; LÚCIO FABIO CALDAS, CBMEG/Unicamp; MARCOS TADEU DOS SANTOS, CBMEG/Unicamp; PAULA REGINA KUSER FALCÃO, CNPTIA; GORAN NESHICH, CNPTIA; LAURA M. M. OTTOBONI, CBMEG/Unicamp.
Appears in Collections:Resumo em anais de congresso (CNPTIA)

Files in This Item:
File Description SizeFormat 
I-95-ISMB-2006.pdf133.41 kBAdobe PDFThumbnail
View/Open

FacebookTwitterDeliciousLinkedInGoogle BookmarksMySpace