Surfactants are commonly used in biopharmaceutical formulations to stabilize proteins against aggregation. However, the choice of a suitable surfactant for a particular protein is decided mostly empirically, and their mechanism of action on molecular level is largely unknown. Here we show that a straightforward label-free method, saturation transfer difference (STD) nuclear magnetic resonance (NMR) spectroscopy, can be used to detect protein-surfactant interactions in formulations of a model...
[NMR paper] Membrane Interactions of alpha-Synuclein Revealed by Multiscale Molecular Dynamics Simulations, Markov State Models, and NMR
Membrane Interactions of alpha-Synuclein Revealed by Multiscale Molecular Dynamics Simulations, Markov State Models, and NMR
?-Synuclein (?S) is a presynaptic protein that binds to cell membranes and is linked to Parkinson's disease (PD). Binding of ?S to membranes is a likely first step in the molecular pathophysiology of PD. The ?S molecule can adopt multiple conformations, being largely disordered in water, adopting a ?-sheet conformation when present in amyloid fibrils, and forming a dynamic multiplicity of ?-helical conformations when bound to lipid bilayers and related...
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[NMR paper] Assessing the Metabolomic Profile of Multiple Sclerosis Patients Treated with Interferon Beta 1a by 1H-NMR Spectroscopy.
Assessing the Metabolomic Profile of Multiple Sclerosis Patients Treated with Interferon Beta 1a by 1H-NMR Spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Assessing the Metabolomic Profile of Multiple Sclerosis Patients Treated with Interferon Beta 1a by 1H-NMR Spectroscopy.
Neurotherapeutics. 2019 07;16(3):797-807
Authors: Lorefice L, Murgia F, Fenu G, Frau J, Coghe G, Murru MR, Tranquilli S, Visconti A, Marrosu MG, Atzori L, Cocco E...
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[NMR paper] Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy.
Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy.
Related Articles Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy.
Biomolecules. 2020 Mar 10;10(3):
Authors: Kim DH, Lee J, Mok KH, Lee JH, Han KH
Abstract
Elucidating the structural details of proteins is highly valuable and important for the proper understanding of protein function. In the case of intrinsically disordered proteins (IDPs), however, obtaining the structural details is quite challenging, as the traditional...
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[NMR paper] New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization.
New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization.
New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization.
FEBS J. 2014 Dec 11;
Authors: Elazari-Shalom H, Shaked H, Esteban-Martin S, Salvatella X, Barda-Saad M, Chill JH
Abstract
WASp-interacting protein (WIP) is an intrinsically disordered 503-residue polypeptide with a key role in actin polymerization in activated T cells. Its interaction with actin is mediated...
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12-17-2014 09:43 PM
Interactions of gemini surfactants with two model proteins: NMR, CD, and fluorescence spectroscopies
Interactions of gemini surfactants with two model proteins: NMR, CD, and fluorescence spectroscopies
1 March 2012
Publication year: 2012
Source:Journal of Colloid and Interface Science, Volume 369, Issue 1</br>
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Gemini surfactants have two polar head groups and two hydrocarbon tails. Compared with conventional surfactants, geminis have much lower (?M vs. mM) critical micelle concentrations and possess slower (ms vs. ?s) monomer ? micelle kinetics. The structure of the gemini surfactants studied is ·2Br- where s =4, 5, or 6. Our objective is to reveal the effect...
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02-03-2013 10:13 AM
[NMR paper] NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformation
NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.
Related Articles NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.
J Biol Chem. 2004 Aug 13;279(33):34963-70
Authors: Santiveri CM, Pérez-Cañadillas JM, Vadivelu MK, Allen MD, Rutherford TJ, Watkins NA, Bycroft M
The structure of alpha-hemoglobin stabilizing protein (AHSP), a molecular chaperone for free alpha-hemoglobin, has been determined using NMR spectroscopy....
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[NMR paper] NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and c
NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Related Articles NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Int J Biol Macromol. 1998 May-Jun;22(3-4):197-209
Authors: Carver JA, Lindner RA
The subunit molecular mass of alpha-crystallin, like many small heat-shock proteins (sHsps), is around 20 kDa although the protein exists as a large aggregate of average mass around 800...
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[NMR paper] The three-dimensional high resolution structure of human interferon alpha-2a determin
The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution.
J Mol Biol. 1997 Dec 12;274(4):661-75
Authors: Klaus W, Gsell B, Labhardt AM, Wipf B, Senn H
The solution structure of recombinant human interferon...
Insights into the stabilization of interferon alpha by two surfactants revealed by STD-NMR spectroscopy
Linear Mode
