[NMR paper] Water dynamics changes and protein denaturation in surf clam evaluated by two-dimensional LF-NMR T1-T2 relaxation technique during heating process.
Related ArticlesWater dynamics changes and protein denaturation in surf clam evaluated by two-dimensional LF-NMR T1-T2 relaxation technique during heating process.
Food Chem. 2020 Mar 16;320:126622
Authors: Wang S, Lin R, Cheng S, Tan M
Abstract
Water dynamics and protein denaturation in surf clam during heating were studied by the two-dimensional low-field nuclear magnetic resonance (LF-NMR) T1-T2 relaxation technique. A significant change was found for clam around 80*°C and direct visualization of the water state change was provided by the magnetic resonance imaging. Principal components and heatmap analysis revealed that clam treated at 80-100*°C located at different region from those treated at 40-70*°C. The clams heated at 80*°C showed a maximum water holding capability, and significant microstructure change. The differential scanning calorimetry analysis indicated a denaturation of protein when the temperature was over 80*°C. The hardness and chewiness had a maximum value at 80 and 70*°C, respectively. The color parameter L* showed a significant increase when temperature was over 80*°C. This demonstrated that the T1-T2 technique has potential in evaluating water dynamics for surf clam during heating.
PMID: 32203840 [PubMed - as supplied by publisher]
Sensitivity-enhanced three-dimensional and carbon-detected two-dimensional NMR of proteins using hyperpolarized water
Sensitivity-enhanced three-dimensional and carbon-detected two-dimensional NMR of proteins using hyperpolarized water
Abstract
Signal enhancements of up to two orders of magnitude in protein NMR can be achieved by employing HDO as a vector to introduce hyperpolarization into folded or intrinsically disordered proteins. In this approach, hyperpolarized HDO produced by dissolution-dynamic nuclear polarization (D-DNP) is mixed with a protein solution waiting in a high-field NMR spectrometer, whereupon amide proton exchange and nuclear Overhauser effects...
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[NMR paper] Ordering effect of protein surfaces on water dynamics: NMR relaxation study.
Ordering effect of protein surfaces on water dynamics: NMR relaxation study.
Ordering effect of protein surfaces on water dynamics: NMR relaxation study.
Biophys Chem. 2019 Apr 08;249:106149
Authors: Bonechi C, Tamasi G, Pardini A, Donati A, Volpi V, Leone G, Consumi M, Magnani A, Rossi C
Abstract
Proteins in solution affect the structural and dynamic properties of the bulk water at the protein-water interface, resulting in a contribution to the order of the hydration water. Theoretical and experimental NMR relaxation methods...
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04-14-2019 10:41 AM
Investigation the effects of protein hydration states on the mobility water and fat in meat batters by LF-NMR technique
Investigation the effects of protein hydration states on the mobility water and fat in meat batters by LF-NMR technique
Publication date: Available online 8 October 2015
Source:LWT - Food Science and Technology</br>
Author(s): Jun-Hua Shao, Ya-Min Deng, Li Song, A. Batur, Na Jia, Deng-Yong Liu</br>
The use of LF-NMR technique for assessing the influence of meat protein hydration states on the mobility water and fat in meat batters was investigated. Three relaxation components, T22 (50 ms), T2b and T21 (lower than 10 ms) were found in meat group and fat...
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10-09-2015 03:05 AM
[NMR paper] Effect of thermal denaturation on water-collagen interactions: NMR relaxation and dif
Effect of thermal denaturation on water-collagen interactions: NMR relaxation and differential scanning calorimetry analysis.
Related Articles Effect of thermal denaturation on water-collagen interactions: NMR relaxation and differential scanning calorimetry analysis.
Biopolymers. 1999 Dec;50(7):690-6
Authors: Rochdi A, Foucat L, Renou JP
The dependence of the proton spin-lattice relaxation rate, and of the enthalpy and temperature of denaturation on water content, were studied by nmr and differential scanning calorimetry (DSC) in native and...
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Hydration water dynamics in biopolymers from NMR relaxation in the rotating frame.
Hydration water dynamics in biopolymers from NMR relaxation in the rotating frame.
Related Articles Hydration water dynamics in biopolymers from NMR relaxation in the rotating frame.
J Magn Reson. 2010 Sep 24;
Authors: Blicharska B, Peemoeller H, Witek M
Assuming dipole-dipole interaction as the dominant relaxation mechanism of protons of water molecules adsorbed onto macromolecule (biopolymer) surfaces we have been able to model the dependences of relaxation rates on temperature and frequency. For adsorbed water molecules the correlation times are...
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[NMR paper] Relaxation study of the backbone dynamics of human profilin by two-dimensional 1H-15N
Relaxation study of the backbone dynamics of human profilin by two-dimensional 1H-15N NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Relaxation study of the backbone dynamics of human profilin by two-dimensional 1H-15N NMR.
FEBS Lett. 1993 Dec 28;336(3):457-61
Authors: Constantine KL, Friedrichs MS, Bell AJ, Lavoie TB, Mueller L, Metzler WJ
The dynamic properties of 111 backbone HN sites in uncomplexed human profilin, a protein of 139 residues, have been...
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[NMR paper] Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H N
Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
Related Articles Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
Biochemistry. 1991 Nov 26;30(47):11313-20
Authors: Tamura A, Kimura K, Akasaka K
Structural transitions of the protein Streptomyces subtilisin inhibitor (SSI) from the native state to the cold-denatured and heat-denatured states were studied by 1H NMR spectroscopy in the temperature range from -10 to 60 degrees C in the acidic pH range....
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08-21-2010 11:12 PM
[NMR paper] Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H N
Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
Related Articles Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
Biochemistry. 1991 Nov 26;30(47):11313-20
Authors: Tamura A, Kimura K, Akasaka K
Structural transitions of the protein Streptomyces subtilisin inhibitor (SSI) from the native state to the cold-denatured and heat-denatured states were studied by 1H NMR spectroscopy in the temperature range from -10 to 60 degrees C in the acidic pH range....
Water dynamics changes and protein denaturation in surf clam evaluated by two-dimensional LF-NMR T1-T2 relaxation technique during heating process.
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