Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Marco Polimeni"'
Autor:
Marco Polimeni, Emanuela Zaccarelli, Alessandro Gulotta, Mikael Lund, Anna Stradner, Peter Schurtenberger
Publikováno v:
APL Bioengineering, Vol 8, Iss 1, Pp 016111-016111-13 (2024)
Developing efficient and robust computational models is essential to improve our understanding of protein solution behavior. This becomes particularly important to tackle the high-concentration regime. In this context, the main challenge is to put fo
Externí odkaz:
https://doaj.org/article/36f51d5e1c4e4207b6c45324845038b0
Autor:
Alina Kulakova, Dillen Augustijn, Inas El Bialy, Lorenzo Gentiluomo, Maria Laura Greco, Stefan Hervø-Hansen, Sowmya Indrakumar, Sujata Mahapatra, Marcello Martinez Morales, Christin Pohl, Marco Polimeni, Aisling Roche, Hristo L. Svilenov, Andreas Tosstorff, Matja Zalar, Robin Curtis, Jeremy P. Derrick, Wolfgang Frieß, Alexander P. Golovanov, Mikael Lund, Allan Nørgaard, Tarik A. Khan, Günther H. J. Peters, Alain Pluen, Dierk Roessner, Werner W. Streicher, Christopher F. van der Walle, Jim Warwicker, Shahid Uddin, Gerhard Winter, Jens Thostrup Bukrinski, Åsmund Rinnan, Pernille Harris
Publikováno v:
Molecular Pharmaceutics.
Autor:
Sujata Mahapatra, Marco Polimeni, Lorenzo Gentiluomo, Dierk Roessner, Wolfgang Frieß, Günther H. J. Peters, Werner W. Streicher, Mikael Lund, Pernille Harris
Publikováno v:
Molecular Pharmaceutics
Using light scattering (LS), small-angle X-ray scattering (SAXS), and coarse-grained Monte Carlo (MC) simulations, we studied the self-interactions of two monoclonal antibodies (mAbs), PPI03 and PPI13. With LS measurements, we obtained the osmotic se
Autor:
Coralie Pasquier, Søren Roi Midtgaard, Marco Polimeni, Christian Isak Jørgensen, Lise Arleth, Thomas H. Callisen, Mikael Lund
Publikováno v:
Pasquier, C, Midtgaard, S R, Polimeni, M, Jorgensen, C I, Arleth, L, Callisen, T H & Lund, M 2023, ' Anisotropic protein-protein interactions in dilute and concentrated solutions ', Journal of Colloid and Interface Science, vol. 629, pp. 794-804 . https://doi.org/10.1016/j.jcis.2022.08.054
Interactions between biomolecules are ubiquitous in nature and crucial to many applications including vaccine development; environmentally friendly textile detergents; and food formulation. Using small angle X-ray scattering and structure-based molec
Publikováno v:
Journal of Chemical Theory and Computation. 16:1843-1853
We present a scheme for transferring conformational degrees of freedom from all-atom (AA) simulations of an intrinsically disordered protein (IDP) to coarse-grained (CG) Monte Carlo (MC) simulations using conformational swap moves. AA simulations of
Publikováno v:
The Journal of chemical physics. 155(19)
The osmotic pressure of dilute electrolyte solutions containing charged macro-ions as well as counterions can be computed directly from the particle distribution via the well-known cell model. Originally derived within the Poisson–Boltzmann mean-fi
Publikováno v:
UEMCON
The goal of the paper is to design and implement a system to measure food waste in Pierce Dining Hall on the campus of Stevens Institute of Technology. The system would likely utilize a camera to identify types of food waste based on a database conta
Publikováno v:
The journal of physical chemistry. B. 121(38)
The interface between biological matter and inorganic materials is a widely investigated research topic due to possible applications in biomedicine and nanotechnology. In this context, the molecular level adsorption mechanism that drives specific rec
The interface between biological matter and inorganic materials is a widely investigated research topic due to possible applications in biomedicine and nanotechnology. In this context, the molecular level adsorption mechanism that drives specific rec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeefb28193e0ed52944f657433b861b0
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85030531577&doi=10.1021/acs.jpcb.7b04707&partnerID=40&md5=cd4096f12c2834c9285a58e52e537520
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85030531577&doi=10.1021/acs.jpcb.7b04707&partnerID=40&md5=cd4096f12c2834c9285a58e52e537520