Related ArticlesChanges in orcine muscle water characteristics during growth--an in vitro low-field NMR relaxation study.
J Magn Reson. 2002 Aug;157(2):267-76
Authors: Bertram HC, Rasmussen M, Busk H, Oksbjerg N, Karlsson AH, Andersen HJ
This study investigates the effects of developmental stage and muscle type on the mobility and distribution of water within skeletal muscles, using low-field (1)H-NMR transverse relaxation measurements in vitro on four different porcine muscles (M. longissimus dorsi, M. semitendinosus, M. biceps femoris, M. vastus intermedius) from a total of 48 pigs slaughtered at various weight classes between 25 kg and 150 kg. Principal component analysis (PCA) revealed effects of both slaughter weight and muscle type on the transverse relaxation decay. Independent of developmental stage and muscle type, distributed exponential analysis of the NMR T(2) relaxation data imparted the existence of three distinct water populations, T(2b), T(21), and T(22), with relaxation times of approximately 1-10, 45-120, and 200-500 ms, respectively. The most profound change during muscle growth was a shift toward faster relaxation in the intermediate time constant, T(21). It decreased by approx. 24% in all four muscle types during the period from 25 to 150 kg live weight. Determination of dry matter, fat, and protein content in the muscles showed that the changes in relaxation time of the intermediate time constant, T(21), during growth should be ascribed mainly to a change in protein content, as the protein content explained 77% of the variation in the T(21) time constant. Partial least squares (PLS) regression revealed validated correlations in the region of 0.58 to 0.77 between NMR transverse relaxation data and muscle development for all the four muscle types, which indicates that NMR relaxation measurements may be used in the prediction of muscle developmental stage.
Characteristics of zero-quantum correlation spectroscopy in MAS NMR experiments.
Characteristics of zero-quantum correlation spectroscopy in MAS NMR experiments.
Characteristics of zero-quantum correlation spectroscopy in MAS NMR experiments.
J Magn Reson. 2010 Dec;207(2):197-205
Authors: Köneke SG, van Beek JD, Ernst M, Meier BH
Zero-quantum coherence generation and reconversion in magic-angle spinning solid-state NMR is analyzed. Two methods are discussed based on implementations using symmetry-based pulse sequences that utilize either isotropic J couplings or dipolar couplings. In either case, the decoupling of abundant...
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[NMR paper] Yeast expression and NMR analysis of the extracellular domain of muscle nicotinic ace
Yeast expression and NMR analysis of the extracellular domain of muscle nicotinic acetylcholine receptor alpha subunit.
Related Articles Yeast expression and NMR analysis of the extracellular domain of muscle nicotinic acetylcholine receptor alpha subunit.
J Biol Chem. 2002 Apr 12;277(15):12613-21
Authors: Yao Y, Wang J, Viroonchatapan N, Samson A, Chill J, Rothe E, Anglister J, Wang ZZ
The alpha subunit of the nicotinic acetylcholine receptor (AChR) from Torpedo electric organ and mammalian muscle contains high affinity binding sites for...
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11-24-2010 08:49 PM
[NMR paper] Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alp
Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein.
Related Articles Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein.
J Mol Biol. 2001 Sep 28;312(4):833-47
Authors: Greenfield NJ, Huang YJ, Palm T, Swapna GV, Monleon D, Montelione GT, Hitchcock-DeGregori SE
Tropomyosin is an alpha-helical coiled-coil protein that aligns head-to-tail along the length of the actin filament and...
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11-19-2010 08:44 PM
[NMR paper] Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectrosc
Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectroscopy and 31P NMR spectroscopy.
Related Articles Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectroscopy and 31P NMR spectroscopy.
Biochemistry. 2001 Feb 20;40(7):1884-9
Authors: Rohrer M, Prisner TF, Brügmann O, Käss H, Spoerner M, Wittinghofer A, Kalbitzer HR
The small GTPase Ras plays a key role as a molecular switch in the intercellular signal transduction. On Mg(2+) --> Mn(2+) substituted samples, the first ligand sphere of...
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11-19-2010 08:32 PM
[NMR paper] 13C/31P NMR assessment of mitochondrial energy coupling in skeletal muscle of awake f
13C/31P NMR assessment of mitochondrial energy coupling in skeletal muscle of awake fed and fasted rats. Relationship with uncoupling protein 3 expression.
Related Articles 13C/31P NMR assessment of mitochondrial energy coupling in skeletal muscle of awake fed and fasted rats. Relationship with uncoupling protein 3 expression.
J Biol Chem. 2000 Dec 15;275(50):39279-86
Authors: Jucker BM, Ren J, Dufour S, Cao X, Previs SF, Cadman KS, Shulman GI
To examine the relationship between mitochondrial energy coupling in skeletal muscle and change in...
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11-19-2010 08:29 PM
[NMR paper] NMR structure and functional characteristics of the hydrophilic N terminus of the pot
NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1.
Related Articles NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1.
J Biol Chem. 1999 Dec 10;274(50):35521-5
Authors: Wissmann R, Baukrowitz T, Kalbacher H, Kalbitzer HR, Ruppersberg JP, Pongs O, Antz C, Fakler B
Rapid N-type inactivation of voltage-dependent potassium (Kv) channels controls membrane excitability and signal propagation in central...
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11-18-2010 08:31 PM
[NMR paper] NMR study of the transforming growth factor-alpha (TGF-alpha)-epidermal growth factor
NMR study of the transforming growth factor-alpha (TGF-alpha)-epidermal growth factor receptor complex. Visualization of human TGF-alpha binding determinants through nuclear Overhauser enhancement analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR study of the transforming growth factor-alpha (TGF-alpha)-epidermal growth factor receptor complex. Visualization of human TGF-alpha binding determinants through nuclear Overhauser enhancement analysis.
J Biol...
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[NMR paper] NMR solution structure of calcium-saturated skeletal muscle troponin C.
NMR solution structure of calcium-saturated skeletal muscle troponin C.
Related Articles NMR solution structure of calcium-saturated skeletal muscle troponin C.
Biochemistry. 1995 Dec 12;34(49):15953-64
Authors: Slupsky CM, Sykes BD
Troponin C (TnC) is an 18 kDa (162-residue) thin-filament calcium-binding protein responsible for triggering muscle contraction upon the release of calcium from the sarcoplasmic reticulum. The structure of TnC with two calcium ions bound has previously been solved by X-ray methods. Shown here is the solution...
Changes in orcine muscle water characteristics during growth--an in vitro low-field N
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