Zobrazeno 1 - 10
of 645
pro vyhledávání: '"Folding funnel"'
Autor:
Murilo N. Sanches, R. Gonzalo Parra, Rafael G. Viegas, Antonio B. Oliveira, Peter G. Wolynes, Diego U. Ferreiro, Vitor B.P. Leite
Publikováno v:
QRB Discovery, Vol 3 (2022)
Ankyrin (ANK) repeat proteins are coded by tandem occurrences of patterns with around 33 amino acids. They often mediate protein–protein interactions in a diversity of biological systems. These proteins have an elongated non-globular shape and ofte
Externí odkaz:
https://doaj.org/article/405f234b982b4658a6e621eeb52ef6c0
Akademický článek
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Publikováno v:
Biomolecules, Vol 10, Iss 2, p 250 (2020)
“How do proteins fold?” Researchers have been studying different aspects of this question for more than 50 years. The most conceptual aspect of the problem is how protein can find the global free energy minimum in a biologically reasonable time,
Externí odkaz:
https://doaj.org/article/b3a65c2e52a340db893911a676da52bb
Akademický článek
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Autor:
Peter Wolynes, Antonio Bento Oliveira Junior, Rafael Giordano Viegas, Rodrigo Gonzalo Parra, Diego Ferreiro, Vitor Leite, Murilo Nogueira Sanches
Publikováno v:
UPCommons. Portal del coneixement obert de la UPC
Universitat Politècnica de Catalunya (UPC)
Universitat Politècnica de Catalunya (UPC)
Ankyrin (ANK) repeat proteins are coded by tandem occurrences of patterns with around 33 amino acids. They often mediate protein–protein interactions in a diversity of biological systems. These proteins have an elongated non-globular shape and ofte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c29d1077fc91ff4edca6eed2ddb60ed
http://hdl.handle.net/2117/371618
http://hdl.handle.net/2117/371618
Autor:
Andrews, Benjamin T., Gosavi, Shachi, Finke, John M., Onuchic, José N., Jennings, Patricia A.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2008 Aug . 105(34), 12283-12288.
Externí odkaz:
https://www.jstor.org/stable/25463851
Publikováno v:
Biomolecules
Biomolecules, Vol 10, Iss 2, p 250 (2020)
Biomolecules, Vol 10, Iss 2, p 250 (2020)
“How do proteins fold?” Researchers have been studying different aspects of this question for more than 50 years. The most conceptual aspect of the problem is how protein can find the global free energy minimum in a biologically reasonable time,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34afe8474babadc76e45b28c4f028a78
http://europepmc.org/articles/PMC7072185
http://europepmc.org/articles/PMC7072185
Variational embedding of protein folding simulations using gaussian mixture variational autoencoders
Publikováno v:
J Chem Phys
Conformational sampling of biomolecules using molecular dynamics simulations often produces large amount of high dimensional data that makes it difficult to interpret using conventional analysis techniques. Dimensionality reduction methods are thus r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0affc976cb351160b4116c337fd2a663
http://arxiv.org/abs/2108.12493
http://arxiv.org/abs/2108.12493
Autor:
Celine Kelso, J. Andrew Aquilina, Justin J. Yerbury, Luke McAlary, S. P. Fitzgerald, Justin L. P. Benesch, Julian A. Harrison
Publikováno v:
Analytical Chemistry. 92:1702-1711
Native mass spectrometry (MS) is a powerful means for studying macromolecular protein assemblies, including accessing activated states. However, much remains to be understood about what governs which regions of the protein (un)folding funnel, which c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c035e7614fb728d052b11954bd385a1c
https://doi.org/10.1021/acs.analchem.9b01699
https://doi.org/10.1021/acs.analchem.9b01699