[NMR paper] Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach.
Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach.
Related Articles Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach.
J Pharm Sci. 2018 Jun 05;:
Authors: Torosantucci R, Furtmann B, Elshorst B, Pfeiffer-Marek S, Hartleb T, Andres N, Bussemer T
Abstract
Preservatives are excipients...
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06-10-2018 03:09 AM
Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach
Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach
Publication date: Available online 5 June 2018
Source:Journal of Pharmaceutical Sciences</br>
Author(s): Riccardo Torosantucci, Britta Furtmann, Bettina Elshorst, Stefania Pfeiffer-Marek, Tanja Hartleb, Nikolaus Andres, Till Bussemer</br>
Preservatives are excipients essentially needed in pharmaceutical multi-dose formulations to prevent microbial growth. Among available...
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06-06-2018 01:40 AM
New findings help explain speedy transported into and out of the cell's nucleus - (e) Science News (press release) (registration)
http://www.bionmr.com//t1.gstatic.com/images?q=tbn:ANd9GcQslNTa5WNlD6fMn84xCpzCZ276c1VuSTmE5Bl_pYC1leTyGCpixsr6WeOlhIVQO8_MHcM6VGQ4
(e) Science News (press release) (registration)
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New findings help explain speedy transported into and out of the cell's nucleus
(e) Science News (press release) (registration)
Using a technique known as nuclear magnetic resonance spectroscopy, the researchers collected atomic-scale information about the behavior of the FG Nups, focusing on Nsp1, the most studied representative of the FG Nups. Normally, proteins fold into ......
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09-20-2015 12:56 PM
Improved Stability and Spectral Quality in Ex Situ Dissolution DNP Using an Improved Transfer Device
From The DNP-NMR Blog:
Improved Stability and Spectral Quality in Ex Situ Dissolution DNP Using an Improved Transfer Device
Katsikis, S., et al., Improved Stability and Spectral Quality in Ex Situ Dissolution DNP Using an Improved Transfer Device. Appl. Magn. Reson., 2015. 46(7): p. 723-729.
http://dx.doi.org/10.1007/s00723-015-0680-5
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09-07-2015 08:08 PM
[NMR paper] Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
J Biomol NMR. 2014 Jan 4;
Authors: Kovacs H, Gossert A
Abstract
Three improved (13)C-spinlock experiments for side chain assignments of...
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01-07-2014 11:16 PM
[NMR paper] ?2 -Adrenergic Receptor Activation by Agonists Studied with (19) F NMR Spectroscopy.
?2 -Adrenergic Receptor Activation by Agonists Studied with (19) F NMR Spectroscopy.
?2 -Adrenergic Receptor Activation by Agonists Studied with (19) F NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Aug 16;
Authors: Horst R, Liu JJ, Stevens RC, Wüthrich K
Abstract
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08-21-2013 08:49 PM
[NMR paper] Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone ?, ? and side-chain ?(1) and ?(2) dihedral angles.
Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone ?, ? and side-chain ?(1) and ?(2) dihedral angles.
Related Articles Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone ?, ? and side-chain ?(1) and ?(2) dihedral angles.
J Chem Theory Comput. 2012 Sep 11;8(9):3257-3273
Authors: Best RB, Zhu X, Shim J, Lopes PE, Mittal J, Feig M, Mackerell AD
Abstract
While the quality of the current CHARMM22/CMAP additive force field for...
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02-03-2013 10:19 AM
[NMR paper] Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic t
Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
Related Articles Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
J Biomol NMR. 2005 Apr;31(4):279-93
Authors: Gammeren AJ, Hulsbergen FB, Hollander JG, Groot HJ
This study reports the sequence specific chemical shifts...
Low intrinsic efficacy for G protein activation can explain the improved side effect profiles of new opioid agonists - Science
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