Publication date: Available online 20 April 2016 Source:Food Hydrocolloids
Author(s): Birgit Dekkers, Daan W. De Kort, Katarzyna J. Grabowska, Bei Tian, Henk Van As, Atze Jan Van der Goot
We present a combined time domain NMR and rheology approach to quantify the water distribution in a phase separated protein blend. The approach forms the basis for a new tool to assess the microstructural properties of phase separated biopolymer blends, making it highly relevant for many food and non-food related applications. First, we determine the relaxation rate of absorbed water, and the viscoelastic properties of the separated phases as function of the water content. Next, the same properties are measured for the protein blends. Finally, predictions for water distribution obtained from rheological experiments are made via the polymer blending law, and compared to a more direct assessment of the water distribution with time-domain NMR relaxometry (TD-NMR). In this study, the protein blend consists of soy protein isolate (SPI) and vital wheat gluten (WG). We demonstrate that predictions for water distribution are similar for both TD-NMR and rheological measurements. It turns out that water does not distribute homogenously over the phases. Independent of the SPI and WG ratio, more water is absorbed by the SPI phase relative to the WG phase, which largely determines the resulting rheological properties of the blends. Graphical abstract
Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets
Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets
Wan-Na Chen, Christoph Nitsche, Kala Bharath Pilla, Bim Graham, Thomas Huber, Christian D. Klein and Gottfried Otting
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b00416/20160324/images/medium/ja-2016-004167_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b00416
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[NMR paper] Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets.
Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets.
Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets.
J Am Chem Soc. 2016 Mar 14;
Authors: Chen WN, Nitsche C, Pilla KB, Graham B, Huber T, Klein CD, Otting G
Abstract
Structure-guided drug design relies on detailed structural knowledge of protein-ligand complexes, but crystallization of co-complexes is not always possible. Here we present a sensitive nuclear...
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03-15-2016 11:57 AM
[NMR paper] Lipid binding protein response to a bile acid library: a combined NMR and statistical approach.
Lipid binding protein response to a bile acid library: a combined NMR and statistical approach.
Related Articles Lipid binding protein response to a bile acid library: a combined NMR and statistical approach.
FEBS J. 2015 Aug 11;
Authors: Tomaselli S, Pagano K, Boulton S, Zanzoni S, Melacini G, Molinari H, Ragona L
Abstract
Primary bile acids, differing in the hydroxylation pattern, are synthesized from cholesterol in the liver and, once formed, can undergo extensive enzyme-catalyzed glycine/taurine conjugation, giving rise to a...
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[NMR paper] A Combined NMR and Computational Approach to Investigate Peptide Binding to a Designed Armadillo Repeat Protein.
A Combined NMR and Computational Approach to Investigate Peptide Binding to a Designed Armadillo Repeat Protein.
A Combined NMR and Computational Approach to Investigate Peptide Binding to a Designed Armadillo Repeat Protein.
J Mol Biol. 2015 Mar 24;
Authors: Ewald C, Christen MT, Watson RP, Mihajlovic M, Zhou T, Honegger A, Plückthun A, Caflisch A, Zerbe O
Abstract
The specific recognition of peptide sequences by proteins plays an important role both in biology and in diagnostic applications. Here we characterize the...
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A Combined NMR and Computational Approach to Investigate Peptide Binding to a Designed Armadillo Repeat Protein
A Combined NMR and Computational Approach to Investigate Peptide Binding to a Designed Armadillo Repeat Protein
Publication date: Available online 24 March 2015
Source:Journal of Molecular Biology</br>
Author(s): Christina Ewald , Martin T. Christen , Randall P. Watson , Maja Mihajlovic , Ting Zhou , Annemarie Honegger , Andreas Plückthun , Amedeo Caflisch , Oliver Zerbe</br>
The specific recognition of peptide sequences by proteins plays an important role both in biology and in diagnostic applications. Here we characterize the relatively weak binding of the...
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Determining the EnergyLandscape of Proteins by aFast Isotope Exchange NMR Approach
Determining the EnergyLandscape of Proteins by aFast Isotope Exchange NMR Approach
Enrico Rennella, Alessandra Corazza, Luca Codutti, Vittorio Bellotti, Monica Stoppini, Paolo Viglino, Federico Fogolari and Gennaro Esposito
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja209004q/aop/images/medium/ja-2011-09004q_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja209004q
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[NMR paper] Combined frequency- and time-domain NMR spectroscopy. Application to fast protein res
Combined frequency- and time-domain NMR spectroscopy. Application to fast protein resonance assignment.
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J Biomol NMR. 2004 May;29(1):57-64
Authors: Brutscher B
A simple and general method is presented to simplify multi-dimensional NMR spectra of isotope-labeled bio-molecules. The approach is based on band-selective Hadamard-type frequency encoding, which disperses the correlation peaks into different sub-spectra. This makes...
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[NMR paper] Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optic
Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy.
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J Mol Biol. 1998 Feb 27;276(3):657-67
Authors: Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM
The refolding kinetics of the chemically denatured SH3 domain of phosphatidylinositol 3'-kinase (PI3-SH3) have been monitored by real-time one-dimensional 1H NMR coupled with a variety of other biophysical techniques. These...
A combined rheology and time domain NMR approach for determining water distribution in protein blends
Linear Mode
