Protein-based biopharmaceutical drugs, such as monoclonal antibodies, account for the majority of the best-selling drugs globally in recent years. For bioprocesses, key performance indicators are the concentration and aggregate level for the product being produced. In water NMR (wNMR), the use of the water transverse relaxation rate [R(2)(¹H(2)O)] has been previously used to determine protein concentration and aggregate level; however, it cannot be used to separate between them without using an...
Concentration-dependent changes to diffusion and chemical shift of internal standard molecules in aqueous and micellar solutions
Concentration-dependent changes to diffusion and chemical shift of internal standard molecules in aqueous and micellar solutions
Abstract
Sodium 4,4-dimethyl-4-silapentane-1-sulfonate (DSS) is the most widely accepted internal standard for protein NMR studies in aqueous conditions. Since its introduction as a reference standard, however, concerns have been raised surrounding its propensity to interact with biological molecules through electrostatic and hydrophobic interactions. While DSS has been shown to interact with certain proteins, membrane...
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06-06-2018 01:42 PM
Nanometer-scale water- and proton-diffusion heterogeneities across water channels in polymer electrolyte membranes
From The DNP-NMR Blog:
Nanometer-scale water- and proton-diffusion heterogeneities across water channels in polymer electrolyte membranes
Song, J., O.H. Han, and S. Han, Nanometer-scale water- and proton-diffusion heterogeneities across water channels in polymer electrolyte membranes. Angew Chem Int Ed Engl, 2015. 54(12): p. 3615-20.
http://www.ncbi.nlm.nih.gov/pubmed/25630609
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09-25-2015 09:05 AM
[NMR paper] Effects of solvent concentration and composition on protein dynamics: 13C MAS NMR studies of elastin in glycerol-water mixtures.
Effects of solvent concentration and composition on protein dynamics: 13C MAS NMR studies of elastin in glycerol-water mixtures.
Related Articles Effects of solvent concentration and composition on protein dynamics: 13C MAS NMR studies of elastin in glycerol-water mixtures.
Biochim Biophys Acta. 2015 Apr 24;
Authors: Demuth D, Haase N, Malzacher D, Vogel M
Abstract
We use 13C CP MAS NMR to investigate the dependence of elastin dynamics on the concentration and composition of the solvent at various temperatures. For elastin in...
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04-29-2015 03:49 PM
Effects of solvent concentration and composition on protein dynamics: 13C MAS NMR studies of elastin in glycerol-water mixtures
Effects of solvent concentration and composition on protein dynamics: 13C MAS NMR studies of elastin in glycerol-water mixtures
Publication date: Available online 25 April 2015
Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics</br>
Author(s): Dominik Demuth , Nils Haase , Daniel Malzacher , Michael Vogel</br>
We use 13C CP MAS NMR to investigate the dependence of elastin dynamics on the concentration and composition of the solvent at various temperatures. For elastin in pure glycerol, line-shape analysis shows that larger-scale fluctuations of...
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04-26-2015 03:28 AM
PFG-NMR self-diffusion in casein dispersions: Effects of probe size and protein aggregate size
PFG-NMR self-diffusion in casein dispersions: Effects of probe size and protein aggregate size
June 2013
Publication year: 2013
Source:Food Hydrocolloids, Volume 31, Issue 2</br>
</br>
The self-diffusion coefficients of different molecular weight PEGs (Polyethylene glycol) and casein particles were measured, using a pulsed-gradient nuclear magnetic resonance technique (PFG-NMR), in native phosphocaseinate (NPC) and sodium caseinate (SC) dispersions where caseins are not structured into micelles. The dependence of the PEG self-diffusion coefficient on the PEG size, casein...
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02-03-2013 10:05 AM
[NMR paper] NMR relaxation and water self-diffusion studies in whey protein solutions and gels.
NMR relaxation and water self-diffusion studies in whey protein solutions and gels.
Related Articles NMR relaxation and water self-diffusion studies in whey protein solutions and gels.
J Agric Food Chem. 2005 Aug 24;53(17):6784-90
Authors: Colsenet R, Mariette F, Cambert M
The changes in water proton transverse relaxation behavior induced by aggregation of whey proteins are explained in terms of the simple molecular processes of diffusion and chemical exchange. The water self-diffusion coefficient was measured in whey protein solutions and...
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12-01-2010 06:56 PM
[NMR paper] Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by N
Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by NMR.
Related Articles Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by NMR.
J Biomol NMR. 2001 Jun;20(2):111-26
Authors: Gruschus JM, Ferretti JA
Hydration site lifetimes of slowly diffusing water molecules at the protein/DNA interface of the vnd/NK-2 homeodomain DNA complex were determined using novel three-dimensional NMR techniques. The lifetimes were calculated using the ratios of ROE and NOE cross-relaxation rates between...
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11-19-2010 08:32 PM
[NMR paper] Quantitative evaluation of water content in a solid protein by deuterium NMR.
Quantitative evaluation of water content in a solid protein by deuterium NMR.
Related Articles Quantitative evaluation of water content in a solid protein by deuterium NMR.
Biochim Biophys Acta. 1992 Feb 26;1119(2):178-84
Authors: Tamura A, Akasaka K
A method for evaluating absolute water content in a solid protein based on deuterium NMR measurements in solution is described. By dissolving the hydrated solid protein, which has been specifically deuterium-labeled, into deuterium-depleted water and by comparing the deuterium NMR signal intensity...
Decoupling Protein Concentration and Aggregate Content Using Diffusion and Water NMR
Linear Mode
