Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Protein design and engineering"'
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 11 (2023)
Externí odkaz:
https://doaj.org/article/f3c077f01952489591d8ac94f0bb1998
Autor:
Ratul Chowdhury
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 10 (2023)
Externí odkaz:
https://doaj.org/article/0b914b1da23d4bd88f2b762b68f6928c
Autor:
Jalil Villalobos-Alva, Luis Ochoa-Toledo, Mario Javier Villalobos-Alva, Atocha Aliseda, Fernando Pérez-Escamirosa, Nelly F. Altamirano-Bustamante, Francine Ochoa-Fernández, Ricardo Zamora-Solís, Sebastián Villalobos-Alva, Cristina Revilla-Monsalve, Nicolás Kemper-Valverde, Myriam M. Altamirano-Bustamante
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 10 (2022)
Proteins are some of the most fascinating and challenging molecules in the universe, and they pose a big challenge for artificial intelligence. The implementation of machine learning/AI in protein science gives rise to a world of knowledge adventures
Externí odkaz:
https://doaj.org/article/8e8e60e57969460994a513e490c6b1cd
Autor:
Ognjen Perišić, Willy Wriggers
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
We employed mutual information (MI) analysis to detect motions affecting the mechanical resistance of the human-engineered protein Top7. The results are based on the MI analysis of pair contact correlations measured in steered molecular dynamics (SMD
Externí odkaz:
https://doaj.org/article/05229a5b93a24108bfbcfe9deb0ff950
Autor:
Rachel L. Johnson, Hayley G. Blaber, Tomas Evans, Harley L. Worthy, Jacob R. Pope, D. Dafydd Jones
Publikováno v:
Frontiers in Chemistry, Vol 9 (2021)
The formation of protein complexes is central to biology, with oligomeric proteins more prevalent than monomers. The coupling of functionally and even structurally distinct protein units can lead to new functional properties not accessible by monomer
Externí odkaz:
https://doaj.org/article/5fc1cc52946046d5a53248b0cc84651c
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 8 (2020)
Software to predict the change in protein stability upon point mutation is a valuable tool for a number of biotechnological and scientific problems. To facilitate the development of such software and provide easy access to the available experimental
Externí odkaz:
https://doaj.org/article/6a57cf1cc4e54949842811cb411bb880
Autor:
Hermann, Johannes
Crystallization of alcohol dehydrogenase from Lactobacillus brevis and mutants was modeled in silico. Neutron and X-ray crystallography allowed the generation of valid crystal structure models as input for subsequent molecular dynamics free energy si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______518::e921ece73a9b924db626afcb2e2aa023
https://mediatum.ub.tum.de/doc/1579462/document.pdf
https://mediatum.ub.tum.de/doc/1579462/document.pdf
Autor:
Basauri Penagos, Arantza
Publikováno v:
UCrea Repositorio Abierto de la Universidad de Cantabria
Universidad de Cantabria (UC)
Universidad de Cantabria (UC)
Lipopolysaccharide (LPS), or endotoxin, is the main component of the outer membrane of Gram-negative bacteria where lipid A is the responsible segment for its toxicity. It poses a serious risk when detected both in different industries and environmen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=RECOLECTA___::c73cfa602ab4ef8f5fc30eb92e6f42d1
http://hdl.handle.net/10902/21926
http://hdl.handle.net/10902/21926
Autor:
Qin Fu, Tyler D. Moeller, Sudhanshu Shanker, Xiaolu Zheng, Thapakorn Jaroentomeechai, Mingji Li, Ilkay Koçer, Josef Byrne, Emily C. Cox, Sheng Zhang, Sophia W. Hulbert, Jeffrey J. Gray, Matthew P. DeLisa, Jason W. Labonte
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Asparagine-linked (N-linked) protein glycosylation—the covalent attachment of complex sugars to the nitrogen atom in asparagine side chains—is the most widespread posttranslational modification to proteins and also the most complex.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::598ba4b021c4e1604116a0eced8ccbd1
https://doi.org/10.1101/2020.06.28.176198
https://doi.org/10.1101/2020.06.28.176198
Publikováno v:
Frontiers in Bioengineering and Biotechnology
Frontiers in Bioengineering and Biotechnology, Vol 8 (2020)
Frontiers in Bioengineering and Biotechnology, Vol 8 (2020)
Software to predict the change in protein stability upon point mutation is a valuable tool for a number of biotechnological and scientific problems. To facilitate the development of such software and provide easy access to the available experimental
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d9261074995237e576ea900fd0a8577
https://pubmed.ncbi.nlm.nih.gov/33134287
https://pubmed.ncbi.nlm.nih.gov/33134287