Influence of the incorporation of fibers in biscuit dough on proton mobility characterized by time domain NMR.
Food Chem. 2016 Feb 1;192:950-7
Authors: Serial MR, Blanco Canalis MS, Carpinella M, Valentinuzzi MC, León AE, Ribotta PD, Acosta RH
Abstract
The effect of fiber addition on the distribution and mobility of protons in biscuits is studied by using low resolution time domain nuclear magnetic resonance (TD-NMR). The proportion of flour is reduced in order to incorporate inulin and oat fiber. NMR temperature dependent experiments are carried out in order to gain insight on the processes occurring in biscuit baking. Proton populations were identified measuring spin-spin relaxation times (T2). The major change in the relaxation profiles upon incorporation of fibers corresponds to mobile water molecules, which appear to be related to dough spreading behavior and biscuit quality. Biscuit samples baked in a commercial oven were studied by two dimensional spin-lattice/spin-spin (T1-T2) relaxation maps. The T1/T2 ratio is used as an indicator of the population mobility, where changes in the mobility of water in contact with flour components as starch, proteins and pentosans are observed.
[NMR paper] Real-time kinetics of high-mobility group box 1 oxidation in extracellular fluids studied by in situ protein NMR spectroscopy.
Real-time kinetics of high-mobility group box 1 oxidation in extracellular fluids studied by in situ protein NMR spectroscopy.
Real-time kinetics of high-mobility group box 1 oxidation in extracellular fluids studied by in situ protein NMR spectroscopy.
J Biol Chem. 2013 Feb 27;
Authors: Zandarashvili L, Sahu D, Lee K, Lee YS, Singh P, Rajarathnam K, Iwahara J
Abstract
Some extracellular proteins are initially secreted in the reduced form via a non-canonical pathway bypassing the endoplasmic reticulum, and become oxidized in the...
nmrlearner
Journal club
0
03-01-2013 09:57 PM
[NMR paper] The cellular prion protein traps Alzheimer's A? in an oligomeric form and disassembles amyloid fibers.
The cellular prion protein traps Alzheimer's A? in an oligomeric form and disassembles amyloid fibers.
Related Articles The cellular prion protein traps Alzheimer's A? in an oligomeric form and disassembles amyloid fibers.
FASEB J. 2013 Jan 30;
Authors: Younan ND, Sarell CJ, Davies P, Brown DR, Viles JH
Abstract
There is now strong evidence to show that the presence of the cellular prion protein (PrP(C)) mediates amyloid-? (A?) neurotoxicity in Alzheimer's disease (AD). Here, we probe the molecular details of the interaction between PrP(C)...
nmrlearner
Journal club
0
02-03-2013 10:19 AM
Probing Cation and VacancyOrdering in the Dry andHydrated Yttrium-Substituted BaSnO3 Perovskite by NMR Spectroscopyand First Principles Calculations: Implications for Proton Mobility
Probing Cation and VacancyOrdering in the Dry andHydrated Yttrium-Substituted BaSnO3 Perovskite by NMR Spectroscopyand First Principles Calculations: Implications for Proton Mobility
Lucienne Buannic, Fre?de?ric Blanc, Derek S. Middlemiss and Clare P. Grey
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja304712v/aop/images/medium/ja-2012-04712v_0012.gif
Journal of the American Chemical Society
DOI: 10.1021/ja304712v
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/L9351EyeKM8
nmrlearner
Journal club
0
08-24-2012 06:42 AM
Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR.
Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR.
Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR.
Proc Natl Acad Sci U S A. 2011 May 31;108(22):E169-76
Authors: Takayama Y, Clore GM
Abstract
The intra- and intermolecular translocation processes whereby the bi-domain transcription factor Oct1 searches for its specific DNA target site have been investigated by...
nmrlearner
Journal club
1
08-25-2011 07:02 AM
Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR [Biophysics and Computational Biology]
Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR
Takayama, Y., Clore, G. M....
Date: 2011-05-31
The intra- and intermolecular translocation processes whereby the bi-domain transcription factor Oct1 searches for its specific DNA target site have been investigated by residual dipolar coupling (RDC) and paramagnetic relaxation enhancement (PRE) measurements. The RDC data show that the orientation of the POUS and POUHD domains of Oct1 relative to the long axis of the DNA is the same for specific and...
nmrlearner
Journal club
0
05-31-2011 11:41 PM
[NMR paper] Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interact
Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD.
Related Articles Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD.
Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):709-14
Authors: Bann JG, Pinkner J, Hultgren SJ, Frieden C
PapD is a periplasmic chaperone essential for P pilus formation in pyelonephritic strains of E. coli. It is composed of two domains, each of which contains a tryptophan...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[Stan NMR blog] Compact permanent magnets for time-domain NMR
Compact permanent magnets for time-domain NMR
Compact MR-quality permanent magnets available off the shelf up to 0.5 T
More...
nmrlearner
News from NMR blogs
0
08-21-2010 05:42 PM
Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Si
Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Site-Specific NMR Relaxation Rates.
Related Articles Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Site-Specific NMR Relaxation Rates.
J Am Chem Soc. 2010 Aug 6;
Authors: Krushelnitsky A, Zinkevich T, Reichert D, Chevelkov V, Reif B
For the first time, we have demonstrated the site-resolved measurement of reliable (i.e., free of interfering effects) (15)N R(1rho) relaxation rates from a solid protein to extract dynamic...
Influence of the incorporation of fibers in biscuit dough on proton mobility characterized by time domain NMR.
Linear Mode
