The energy cost of polypeptide knot formation and its folding consequences
Descripción del Articulo
This work was supported by Fondecyt 11110534 (to M.B.), 1151274 (to M.B.), 11130263 (to C.A.M.W.), Anillo 1107 (to M.B.), and Chile and Fondecyt 196–2013 (to D.G.G.) CONCYTEC, Perú. This research was partially supported by the supercomputing infrastructure of the NLHPC (ECM-02) at Universidad de Chi...
| Autores: | , , , , , , |
|---|---|
| Formato: | artículo |
| Fecha de Publicación: | 2017 |
| Institución: | Consejo Nacional de Ciencia Tecnología e Innovación |
| Repositorio: | CONCYTEC-Institucional |
| Lenguaje: | inglés |
| OAI Identifier: | oai:repositorio.concytec.gob.pe:20.500.12390/638 |
| Enlace del recurso: | https://hdl.handle.net/20.500.12390/638 https://doi.org/10.1038/s41467-017-01691-1 |
| Nivel de acceso: | acceso abierto |
| Materia: | viral protein polypeptide kinetics Monte Carlo analysis peptide polymer https://purl.org/pe-repo/ocde/ford#1.04.00 |
| id |
CONC_0df6d67888a06f798c240cb205812b64 |
|---|---|
| oai_identifier_str |
oai:repositorio.concytec.gob.pe:20.500.12390/638 |
| network_acronym_str |
CONC |
| network_name_str |
CONCYTEC-Institucional |
| repository_id_str |
4689 |
| dc.title.none.fl_str_mv |
The energy cost of polypeptide knot formation and its folding consequences |
| title |
The energy cost of polypeptide knot formation and its folding consequences |
| spellingShingle |
The energy cost of polypeptide knot formation and its folding consequences Bustamante A. viral protein polypeptide kinetics Monte Carlo analysis peptide peptide polymer https://purl.org/pe-repo/ocde/ford#1.04.00 |
| title_short |
The energy cost of polypeptide knot formation and its folding consequences |
| title_full |
The energy cost of polypeptide knot formation and its folding consequences |
| title_fullStr |
The energy cost of polypeptide knot formation and its folding consequences |
| title_full_unstemmed |
The energy cost of polypeptide knot formation and its folding consequences |
| title_sort |
The energy cost of polypeptide knot formation and its folding consequences |
| author |
Bustamante A. |
| author_facet |
Bustamante A. Sotelo-Campos J. Guerra D.G. Floor M. Wilson C.M.A. Bustamante C. Báez M. |
| author_role |
author |
| author2 |
Sotelo-Campos J. Guerra D.G. Floor M. Wilson C.M.A. Bustamante C. Báez M. |
| author2_role |
author author author author author author |
| dc.contributor.author.fl_str_mv |
Bustamante A. Sotelo-Campos J. Guerra D.G. Floor M. Wilson C.M.A. Bustamante C. Báez M. |
| dc.subject.none.fl_str_mv |
viral protein |
| topic |
viral protein polypeptide kinetics Monte Carlo analysis peptide peptide polymer https://purl.org/pe-repo/ocde/ford#1.04.00 |
| dc.subject.es_PE.fl_str_mv |
polypeptide kinetics Monte Carlo analysis peptide peptide polymer |
| dc.subject.ocde.none.fl_str_mv |
https://purl.org/pe-repo/ocde/ford#1.04.00 |
| description |
This work was supported by Fondecyt 11110534 (to M.B.), 1151274 (to M.B.), 11130263 (to C.A.M.W.), Anillo 1107 (to M.B.), and Chile and Fondecyt 196–2013 (to D.G.G.) CONCYTEC, Perú. This research was partially supported by the supercomputing infrastructure of the NLHPC (ECM-02) at Universidad de Chile. A.B. was supported by Conicyt master fellowship 22121199. We gratefully acknowledge Professor Alexander Vologodskii from New York University for helpful comments and advice. Travel for C.B. to and from Chile and Peru was also partially supported by the Howard Hughes Medical Institute, NIH grant R01GM032543, and the U.S. Department of Energy Office of Basic Energy Sciences Nanomachine Program under contract no. DE-AC02-05CH11231. |
| publishDate |
2017 |
| dc.date.accessioned.none.fl_str_mv |
2024-05-30T23:13:38Z |
| dc.date.available.none.fl_str_mv |
2024-05-30T23:13:38Z |
| dc.date.issued.fl_str_mv |
2017 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article |
| format |
article |
| dc.identifier.uri.none.fl_str_mv |
https://hdl.handle.net/20.500.12390/638 |
| dc.identifier.doi.none.fl_str_mv |
https://doi.org/10.1038/s41467-017-01691-1 |
| dc.identifier.scopus.none.fl_str_mv |
2-s2.0-85034414239 |
| url |
https://hdl.handle.net/20.500.12390/638 https://doi.org/10.1038/s41467-017-01691-1 |
| identifier_str_mv |
2-s2.0-85034414239 |
| dc.language.iso.none.fl_str_mv |
eng |
| language |
eng |
| dc.relation.ispartof.none.fl_str_mv |
Nature Communications |
| dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess |
| dc.rights.uri.none.fl_str_mv |
http://creativecommons.org/licenses/by/4.0/ |
| eu_rights_str_mv |
openAccess |
| rights_invalid_str_mv |
http://creativecommons.org/licenses/by/4.0/ |
| dc.publisher.none.fl_str_mv |
Nature Publishing Group |
| publisher.none.fl_str_mv |
Nature Publishing Group |
| dc.source.none.fl_str_mv |
reponame:CONCYTEC-Institucional instname:Consejo Nacional de Ciencia Tecnología e Innovación instacron:CONCYTEC |
| instname_str |
Consejo Nacional de Ciencia Tecnología e Innovación |
| instacron_str |
CONCYTEC |
| institution |
CONCYTEC |
| reponame_str |
CONCYTEC-Institucional |
| collection |
CONCYTEC-Institucional |
| repository.name.fl_str_mv |
Repositorio Institucional CONCYTEC |
| repository.mail.fl_str_mv |
repositorio@concytec.gob.pe |
| _version_ |
1844883037728276480 |
| spelling |
Publicationrp01312600rp01317600rp01316600rp01313600rp01315600rp01318600rp01314600Bustamante A.Sotelo-Campos J.Guerra D.G.Floor M.Wilson C.M.A.Bustamante C.Báez M.2024-05-30T23:13:38Z2024-05-30T23:13:38Z2017https://hdl.handle.net/20.500.12390/638https://doi.org/10.1038/s41467-017-01691-12-s2.0-85034414239This work was supported by Fondecyt 11110534 (to M.B.), 1151274 (to M.B.), 11130263 (to C.A.M.W.), Anillo 1107 (to M.B.), and Chile and Fondecyt 196–2013 (to D.G.G.) CONCYTEC, Perú. This research was partially supported by the supercomputing infrastructure of the NLHPC (ECM-02) at Universidad de Chile. A.B. was supported by Conicyt master fellowship 22121199. We gratefully acknowledge Professor Alexander Vologodskii from New York University for helpful comments and advice. Travel for C.B. to and from Chile and Peru was also partially supported by the Howard Hughes Medical Institute, NIH grant R01GM032543, and the U.S. Department of Energy Office of Basic Energy Sciences Nanomachine Program under contract no. DE-AC02-05CH11231.Knots are natural topologies of chains. Yet, little is known about spontaneous knot formation in a polypeptide chain—an event that can potentially impair its folding—and about the effect of a knot on the stability and folding kinetics of a protein. Here we used optical tweezers to show that the free energy cost to form a trefoil knot in the denatured state of a polypeptide chain of 120 residues is 5.8 ± 1 kcal mol−1. Monte Carlo dynamics of random chains predict this value, indicating that the free energy cost of knot formation is of entropic origin. This cost is predicted to remain above 3 kcal mol−1 for denatured proteins as large as 900 residues. Therefore, we conclude that naturally knotted proteins cannot attain their knot randomly in the unfolded state but must pay the cost of knotting through contacts along their folding landscape.Fondo Nacional de Desarrollo Científico y Tecnológico - FondecytengNature Publishing GroupNature Communicationsinfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/viral proteinpolypeptide-1kinetics-1Monte Carlo analysis-1peptide-1peptide-1polymer-1https://purl.org/pe-repo/ocde/ford#1.04.00-1The energy cost of polypeptide knot formation and its folding consequencesinfo:eu-repo/semantics/articlereponame:CONCYTEC-Institucionalinstname:Consejo Nacional de Ciencia Tecnología e Innovacióninstacron:CONCYTEC#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#20.500.12390/638oai:repositorio.concytec.gob.pe:20.500.12390/6382024-05-30 15:35:53.442http://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_14cbinfo:eu-repo/semantics/closedAccessmetadata only accesshttps://repositorio.concytec.gob.peRepositorio Institucional CONCYTECrepositorio@concytec.gob.pe#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#<Publication xmlns="https://www.openaire.eu/cerif-profile/1.1/" id="db725cf2-1071-476f-a4da-f74a07e73ee1"> <Type xmlns="https://www.openaire.eu/cerif-profile/vocab/COAR_Publication_Types">http://purl.org/coar/resource_type/c_1843</Type> <Language>eng</Language> <Title>The energy cost of polypeptide knot formation and its folding consequences</Title> <PublishedIn> <Publication> <Title>Nature Communications</Title> </Publication> </PublishedIn> <PublicationDate>2017</PublicationDate> <DOI>https://doi.org/10.1038/s41467-017-01691-1</DOI> <SCP-Number>2-s2.0-85034414239</SCP-Number> <Authors> <Author> <DisplayName>Bustamante A.</DisplayName> <Person id="rp01312" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Sotelo-Campos J.</DisplayName> <Person id="rp01317" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Guerra D.G.</DisplayName> <Person id="rp01316" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Floor M.</DisplayName> <Person id="rp01313" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Wilson C.M.A.</DisplayName> <Person id="rp01315" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Bustamante C.</DisplayName> <Person id="rp01318" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Báez M.</DisplayName> <Person id="rp01314" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> </Authors> <Editors> </Editors> <Publishers> <Publisher> <DisplayName>Nature Publishing Group</DisplayName> <OrgUnit /> </Publisher> </Publishers> <License>http://creativecommons.org/licenses/by/4.0/</License> <Keyword>viral protein</Keyword> <Keyword>polypeptide</Keyword> <Keyword>kinetics</Keyword> <Keyword>Monte Carlo analysis</Keyword> <Keyword>peptide</Keyword> <Keyword>peptide</Keyword> <Keyword>polymer</Keyword> <Abstract>Knots are natural topologies of chains. Yet, little is known about spontaneous knot formation in a polypeptide chain—an event that can potentially impair its folding—and about the effect of a knot on the stability and folding kinetics of a protein. Here we used optical tweezers to show that the free energy cost to form a trefoil knot in the denatured state of a polypeptide chain of 120 residues is 5.8 ± 1 kcal mol−1. Monte Carlo dynamics of random chains predict this value, indicating that the free energy cost of knot formation is of entropic origin. This cost is predicted to remain above 3 kcal mol−1 for denatured proteins as large as 900 residues. Therefore, we conclude that naturally knotted proteins cannot attain their knot randomly in the unfolded state but must pay the cost of knotting through contacts along their folding landscape.</Abstract> <Access xmlns="http://purl.org/coar/access_right" > </Access> </Publication> -1 |
| score |
13.394457 |
Nota importante:
La información contenida en este registro es de entera responsabilidad de la institución que gestiona el repositorio institucional donde esta contenido este documento o set de datos. El CONCYTEC no se hace responsable por los contenidos (publicaciones y/o datos) accesibles a través del Repositorio Nacional Digital de Ciencia, Tecnología e Innovación de Acceso Abierto (ALICIA).
La información contenida en este registro es de entera responsabilidad de la institución que gestiona el repositorio institucional donde esta contenido este documento o set de datos. El CONCYTEC no se hace responsable por los contenidos (publicaciones y/o datos) accesibles a través del Repositorio Nacional Digital de Ciencia, Tecnología e Innovación de Acceso Abierto (ALICIA).
