Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Maria I. Freiberger"'
Autor:
Maria I. Freiberger, Victoria Ruiz-Serra, Camila Pontes, Miguel Romero-Durana, Pablo Galaz-Davison, Cesar A. Ramírez-Sarmiento, Claudio D. Schuster, Marcelo A. Marti, Peter G. Wolynes, Diego U. Ferreiro, R. Gonzalo Parra, Alfonso Valencia
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Abstract Energetic local frustration offers a biophysical perspective to interpret the effects of sequence variability on protein families. Here we present a methodology to analyze local frustration patterns within protein families and superfamilies
Externí odkaz:
https://doaj.org/article/8a24deca089846af8b9e2382e5a27117
Autor:
Maria I. Freiberger, Victoria I. Ruiz-Serra, Camila Pontes, Miguel Romero-Durana, Pablo Galaz-Davison, Cesar Ramírez-Sarmiento, Claudio D. Schuster, Marcelo A. Marti, Peter G. Wolynes, Diego U. Ferreiro, R. Gonzalo Parra, Alfonso Valencia
Energetic local frustration offers a biophysical perspective to interpret the effects of sequence variability on protein families. Here we present a methodology to analyze local frustration patterns within protein families that allows us to uncover c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::de2623746dd7394559d8d5e62ebcf079
https://doi.org/10.1101/2023.01.25.525527
https://doi.org/10.1101/2023.01.25.525527
Autor:
Maria I. Freiberger, Camila M. Clemente, Eneko Valero, Jorge G. Pombo, Cesar O. Leonetti, Soledad Ravetti, R. Gonzalo Parra, Diego U. Ferreiro
Proteins are evolved polymers that minimize their free energy upon folding to their native states. Still, many folded proteins display energetic conflict between residues in various regions that can be identified as highly frustrated, and these have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7cc619d49173f7c586e766aecf3321f6
https://doi.org/10.1101/2022.12.11.519349
https://doi.org/10.1101/2022.12.11.519349
Publikováno v:
The Journal of Physical Chemistry. B
Disordered proteins frequently serve as interaction hubs involving a constrained variety of partners. Complexes with different partners frequently exhibit distinct binding modes, involving regions that remain disordered in the bound state. While the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab04d0686361b580ba8034b88bb6facd
https://doi.org/10.1021/acs.jpcb.0c11068
https://doi.org/10.1021/acs.jpcb.0c11068
Publikováno v:
Clemente, C.M., Freiberger, M.I., Ravetti, S., Beltramo, Dante Miguel ORCID: https://orcid.org/0000-0002-8198-3525 and Garro, Ariel Gustavo (2021) An in silico analysis of Ibuprofen enantiomers in high concentrations of sodium chloride with SARS-CoV-2 main protease. Journal of Biomolecular Structure and Dynamics, 40 (12). pp. 5653-5664. ISSN 0739-1102
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Journal of Biomolecular Structure and Dynamics
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Journal of Biomolecular Structure and Dynamics
2020 will be remembered worldwide for the outbreak of Coronavirus disease (COVID-19), which quickly spread until it was declared as a global pandemic. The main protease (Mpro) of SARS-CoV-2, a key enzyme in coronavirus, represents an attractive pharm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7cb1e0e052bd975d46a0c3dfc26b8d1
https://www.tandfonline.com/doi/full/10.1080/07391102.2021.1872420
https://www.tandfonline.com/doi/full/10.1080/07391102.2021.1872420
Autor:
Peter G. Wolynes, Per Jemth, Diego U. Ferreiro, Monika Fuxreiter, Stefano Gianni, Maria I. Freiberger
Publikováno v:
Accounts of Chemical Research
Conspectus Are all protein interactions fully optimized? Do suboptimal interactions compromise specificity? What is the functional impact of frustration? Why does evolution not optimize some contacts? Proteins and their complexes are best described a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::520074454b7ac45c4907a9e465d1475b
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-441615
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-441615
Autor:
R. Gonzalo Parra, Atilio O Rausch, Peter G. Wolynes, Diego M. Luna, Leandro G Radusky, Maria I. Freiberger, Diego U. Ferreiro, Cesar O. Leonetti
Publikováno v:
Bioinformatics (Oxford, England).
Summary Once folded, natural protein molecules have few energetic conflicts within their polypeptide chains. Many protein structures do however contain regions where energetic conflicts remain after folding, i.e. they are highly frustrated. These reg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f978bab7f9401809a69f4c7cf8b977f0
https://pubmed.ncbi.nlm.nih.gov/33720293
https://pubmed.ncbi.nlm.nih.gov/33720293
Disordered proteins can fold into a well-defined structure upon binding but these complexes are often fuzzy: the originally disordered partner adopts different binding modes when bound to different partners. Here we perform a systematic analysis of 1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4d873e97c29cde8a91fcf205e9049f67
https://doi.org/10.1101/2020.11.11.378091
https://doi.org/10.1101/2020.11.11.378091
Autor:
Rodrigo Gonzalo Parra, Maria I. Freiberger, Cesar O. Leonetti, Soledad Ravetti, Camila M. Clemente, Diego U. Ferreiro
Publikováno v:
Proceedings of 6th International Electronic Conference on Medicinal Chemistry.
The identification of ligand binding sites in a protein is the key to several applications in the bioinformatics area, such as molecular docking, de novo drug design and structural identification of functional sites. In recent years it has been demon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e0eddfc1d12e15dd0f9ecb66931991eb
https://doi.org/10.3390/ecmc2020-07440
https://doi.org/10.3390/ecmc2020-07440
Publikováno v:
PLoS ONE
PLoS ONE, Vol 15, Iss 6, p e0233865 (2020)
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
PLoS ONE, Vol 15, Iss 6, p e0233865 (2020)
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Ankyrin containing proteins are one of the most abundant repeat protein families present in all extant organisms. They are made with tandem copies of similar amino acid stretches that fold into elongated architectures. Here, we built and curated a da
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d52f09576c4ad99518c752f384661485
https://pubmed.ncbi.nlm.nih.gov/32579546
https://pubmed.ncbi.nlm.nih.gov/32579546