Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Fabio C. Zegarra"'
Publikováno v:
Production Engineering. 16:465-480
Accurate prediction of machine tool wear is an essential part of modern and efficient manufacturing. In recent years, many studies have been carried out using machine learning algorithms, both traditional and deep learning; with the latter ones repor
Publikováno v:
The Journal of Physical Chemistry B. 125:3501-3509
Pseudomonas aeruginosa apoazurin (apo, without the copper cofactor) has a single disulfide bond between residues 3 and 26 and unfolds in a two-state reaction in vitro. The disulfide bond covalently connects the N-termini of β-strands 1 and 3; thereb
Publikováno v:
2021 IEEE Sciences and Humanities International Research Conference (SHIRCON).
Publikováno v:
2021 IEEE XXVIII International Conference on Electronics, Electrical Engineering and Computing (INTERCON).
Prediction of machine tool wear is highly dependent on the quality of the measured data and the ability to extract information from such raw data. These data are presented in the form of time series, which cannot be used directly by conventional mach
Autor:
Dirar Homouz, Margaret S. Cheung, Andrei G. Gasic, Lucas Babel, Pernilla Wittung-Stafshede, Fabio C. Zegarra, Michael Kovermann
Here, we show by solution nuclear magnetic resonance measurements that the urea-unfolded protein apoazurin becomes elongated when the synthetic crowding agent dextran 20 is present, in contrast to the prediction from the macromolecular crowding effec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bea8e410a717cf870fc572584ce5c85b
Publikováno v:
Biophysical Journal. 118:197a
Pseudomonas aeruginosa apoazurin (apo, without the copper cofactor) is a two-state folder that has a single disulfide bond between residues 3 and 26. This bond covalently connects the N-termini of beta-strands 1 and 3; thereby it creates a zero-order
We investigated the impact of hydrodynamic interactions (HI) on protein folding using a coarse-grained model. The extent of the impact of hydrodynamic interactions, whether it accelerates, retards, or has no effect on protein folding, has been contro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67e7bb577f94cef76a6196f1f5b87172
https://europepmc.org/articles/PMC6080349/
https://europepmc.org/articles/PMC6080349/
Autor:
Margaret S. Cheung, Michael Kovermann, Lucas Babel, Andrei G. Gasic, Fabio C. Zegarra, Dirar Homouz, Pernilla Wittung-Stafshede
Publikováno v:
Biophysical Journal. 116:59a
Publikováno v:
Biophysical Journal. 110(3)
The interior of living cells is a highly crowded, complex environment where macromolecules exclude volume impacting the dynamics of protein folding. Experimentalists often utilize synthetic crowding agents to mimic this volume exclusion effect that s
Publikováno v:
Biophysical Journal. 114:52a