Molecular dynamics simulations of signal sequences at a membrane/water interface

Detalhes bibliográficos
Autor(a) principal: Arêas, Elizabeth Pinheiro Gomes
Data de Publicação: 1995
Outros Autores: Pascutti, Pedro Geraldo, Schreier, Shirley, Mundim, Kleber Carlos, Bisch, Paulo Mascarello
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UFBA
Texto Completo: http://www.repositorio.ufba.br/ri/handle/ri/8544
Resumo: p.14885–14892
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spelling Arêas, Elizabeth Pinheiro GomesPascutti, Pedro GeraldoSchreier, ShirleyMundim, Kleber CarlosBisch, Paulo MascarelloArêas, Elizabeth Pinheiro GomesPascutti, Pedro GeraldoSchreier, ShirleyMundim, Kleber CarlosBisch, Paulo Mascarello2013-02-19T16:30:35Z2013-02-19T16:30:35Z19950022-3654http://www.repositorio.ufba.br/ri/handle/ri/8544v. 99, n. 40p.14885–14892A recently developed software has been used to model peptides at a cytoplasdmembrane mimetic environment where the interface is represented by a discontinuity in the dielectric constant. Molecular dynamics and energy minimization procedures available in the program were applied to a wild type and to a 50% active mutant (A78rl) peptide signal sequence of a A E. coli receptor (maltoporin). Modeling has been performed for both random coiled and constrained helical structures. As a general feature, the presence of the dielectric discontinuity induced the movement of the molecules' center of mass toward the interface. A decrease in the energy along interface crossing (from E = 80 to E = 2) was observed and interpreted as an indication of their affinity for the lipid-mimetic phase. Distinct pattems of migration were recognized for each sequence, as well as in different simulated conditions for a same peptide. The random coiled peptides easily cross the interface, showing a tendency to go into the nonpolar phase, whereas constrained helical sequences tend to stay at the interface. Potential barriers and potential wells were identified in the modeling space for constrained helical peptides, which have been shown to be dependent on the peptide primary sequence, on the conformational restrictions imposed, and on the charge state of the peptide terminals.Submitted by Suelen Reis (suelen_suzane@hotmail.com) on 2013-02-18T15:10:16Z No. of bitstreams: 1 AREAS.pdf: 1938181 bytes, checksum: 33b7ddcd4c4df2c603ffbda4d210f57d (MD5)Approved for entry into archive by Fatima Cleômenis Botelho Maria (botelho@ufba.br) on 2013-02-19T16:30:35Z (GMT) No. of bitstreams: 1 AREAS.pdf: 1938181 bytes, checksum: 33b7ddcd4c4df2c603ffbda4d210f57d (MD5)Made available in DSpace on 2013-02-19T16:30:35Z (GMT). No. of bitstreams: 1 AREAS.pdf: 1938181 bytes, checksum: 33b7ddcd4c4df2c603ffbda4d210f57d (MD5) Previous issue date: 1995http://dx.doi.org/10.1021/j100040a044reponame:Repositório Institucional da UFBAinstname:Universidade Federal da Bahia (UFBA)instacron:UFBAMolecular dynamics simulations of signal sequences at a membrane/water interfaceThe Journal of physical chemistryinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleenginfo:eu-repo/semantics/openAccessORIGINALAREAS.pdfAREAS.pdfapplication/pdf1938181https://repositorio.ufba.br/bitstream/ri/8544/1/AREAS.pdf33b7ddcd4c4df2c603ffbda4d210f57dMD51LICENSElicense.txtlicense.txttext/plain1762https://repositorio.ufba.br/bitstream/ri/8544/2/license.txt1b89a9a0548218172d7c829f87a0eab9MD52TEXTAREAS.pdf.txtAREAS.pdf.txtExtracted texttext/plain39706https://repositorio.ufba.br/bitstream/ri/8544/3/AREAS.pdf.txt9ca2869ea7291c40b4c307faa809aebfMD53ri/85442022-07-05 14:03:48.79oai:repositorio.ufba.br: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Repositório InstitucionalPUBhttp://192.188.11.11:8080/oai/requestopendoar:19322022-07-05T17:03:48Repositório Institucional da UFBA - Universidade Federal da Bahia (UFBA)false
dc.title.pt_BR.fl_str_mv Molecular dynamics simulations of signal sequences at a membrane/water interface
dc.title.alternative.pt_BR.fl_str_mv The Journal of physical chemistry
title Molecular dynamics simulations of signal sequences at a membrane/water interface
spellingShingle Molecular dynamics simulations of signal sequences at a membrane/water interface
Arêas, Elizabeth Pinheiro Gomes
title_short Molecular dynamics simulations of signal sequences at a membrane/water interface
title_full Molecular dynamics simulations of signal sequences at a membrane/water interface
title_fullStr Molecular dynamics simulations of signal sequences at a membrane/water interface
title_full_unstemmed Molecular dynamics simulations of signal sequences at a membrane/water interface
title_sort Molecular dynamics simulations of signal sequences at a membrane/water interface
author Arêas, Elizabeth Pinheiro Gomes
author_facet Arêas, Elizabeth Pinheiro Gomes
Pascutti, Pedro Geraldo
Schreier, Shirley
Mundim, Kleber Carlos
Bisch, Paulo Mascarello
author_role author
author2 Pascutti, Pedro Geraldo
Schreier, Shirley
Mundim, Kleber Carlos
Bisch, Paulo Mascarello
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Arêas, Elizabeth Pinheiro Gomes
Pascutti, Pedro Geraldo
Schreier, Shirley
Mundim, Kleber Carlos
Bisch, Paulo Mascarello
Arêas, Elizabeth Pinheiro Gomes
Pascutti, Pedro Geraldo
Schreier, Shirley
Mundim, Kleber Carlos
Bisch, Paulo Mascarello
description p.14885–14892
publishDate 1995
dc.date.issued.fl_str_mv 1995
dc.date.accessioned.fl_str_mv 2013-02-19T16:30:35Z
dc.date.available.fl_str_mv 2013-02-19T16:30:35Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://www.repositorio.ufba.br/ri/handle/ri/8544
dc.identifier.issn.none.fl_str_mv 0022-3654
dc.identifier.number.pt_BR.fl_str_mv v. 99, n. 40
identifier_str_mv 0022-3654
v. 99, n. 40
url http://www.repositorio.ufba.br/ri/handle/ri/8544
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.pt_BR.fl_str_mv http://dx.doi.org/10.1021/j100040a044
dc.source.none.fl_str_mv reponame:Repositório Institucional da UFBA
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reponame_str Repositório Institucional da UFBA
collection Repositório Institucional da UFBA
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