Publication date: Available online 18 September 2014 Source:Food Hydrocolloids
Author(s): Enamul Haque , Bhesh R. Bhandari , Michael J. Gidley , Hilton C. Deeth , Andrew K. Whittaker
Instability of proteins in dry form causes solubility loss of milk protein concentrate (MPC) powder upon ageing. High resolution solid state NMR techniques were used to investigate the changes in molecular structure and dynamics of proteins in MPC with varying moisture content (5.5-16.5% w/w) and storage period. The results indicate a slight higher rigidity of molecular domains of protein molecules of non-aged MPC compared to that of the long aged (at 25°C) MPC. It could be suggested from this observation that long-term storage at high relative humidity (RH) may reduce rigidity of the molecular domains due to interaction with water rather than short-term storage at high RH. This may indicate increased molecular mobility of backbone and side chains of protein molecules due to plasticization during ageing which could facilitate protein-protein interaction and protein denaturation. Graphical abstract
[NMR paper] Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
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J Am Chem Soc. 2011 Mar 14;
Authors: Yang J, Aslimovska L, Glaubitz C
Environmental factors such as temperature, hydration, and lipid bilayer properties are tightly coupled to the dynamics of membrane proteins. So far, site-resolved data visualizing the protein's response to alterations in these factors are rare, and conclusions had to be drawn from dynamic data averaged over the whole protein...
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Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
Jun Yang, Lubica Aslimovska and Clemens Glaubitz
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109766n/aop/images/medium/ja-2010-09766n_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109766n
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http://feeds.feedburner.com/~r/acs/jacsat/~4/VmNlca5pCIw
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Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Biophys J. 2010 Nov 17;99(10):3282-9
Authors: Toraya S, Javkhlantugs N, Mishima D, Nishimura K, Ueda K, Naito A
Bombolitin II (BLT2) is one of the hemolytic heptadecapeptides originally isolated from the venom of a bumblebee. Structure and orientation of BLT2 bound to...
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[NMR paper] Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
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Authors: Andronesi OC, Becker S, Seidel K, Heise H, Young HS, Baldus M
It is shown that molecular structure and dynamics of a uniformly labeled membrane protein can be studied under magic-angle-spinning conditions. For this purpose, dipolar recoupling experiments...
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[NMR paper] Solid-state NMR and rigid body molecular dynamics to determine domain orientations of
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Solid-state NMR spectroscopy, in conjunction with rigid body molecular dynamics calculations, shows that monomeric phospholamban in lipid bilayers has two distinct helical domains, with an interhelical angle...
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[NMR paper] NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
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Basic Life Sci. 1990;56:231-53
Authors: Berliner LJ, Kaptein R, Koga K, Musci G
Change in molecular structure and dynamics of protein in milk protein concentrate powder upon ageing by solid-state carbon NMR
Linear Mode
