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378 related items for PubMed ID: 17451251

  • 1. Myowater dynamics and protein secondary structural changes as affected by heating rate in three pork qualities: a combined FT-IR microspectroscopic and 1H NMR relaxometry study.
    Wu Z, Bertram HC, Böcker U, Ofstad R, Kohler A.
    J Agric Food Chem; 2007 May 16; 55(10):3990-7. PubMed ID: 17451251
    [Abstract] [Full Text] [Related]

  • 2. Heat-induced changes in myofibrillar protein structures and myowater of two pork qualities. A combined FT-IR spectroscopy and low-field NMR relaxometry study.
    Bertram HC, Kohler A, Böcker U, Ofstad R, Andersen HJ.
    J Agric Food Chem; 2006 Mar 08; 54(5):1740-6. PubMed ID: 16506827
    [Abstract] [Full Text] [Related]

  • 3. Influence of aging and salting on protein secondary structures and water distribution in uncooked and cooked pork. A combined FT-IR microspectroscopy and 1H NMR relaxometry study.
    Wu Z, Bertram HC, Kohler A, Böcker U, Ofstad R, Andersen HJ.
    J Agric Food Chem; 2006 Nov 01; 54(22):8589-97. PubMed ID: 17061838
    [Abstract] [Full Text] [Related]

  • 4. Monitoring of denaturation processes in aged beef loin by Fourier transform infrared microspectroscopy.
    Kirschner C, Ofstad R, Skarpeid HJ, Høst V, Kohler A.
    J Agric Food Chem; 2004 Jun 16; 52(12):3920-9. PubMed ID: 15186118
    [Abstract] [Full Text] [Related]

  • 5. Salt-induced changes in pork myofibrillar tissue investigated by FT-IR microspectroscopy and light microscopy.
    Böcker U, Ofstad R, Bertram HC, Egelandsdal B, Kohler A.
    J Agric Food Chem; 2006 Sep 06; 54(18):6733-40. PubMed ID: 16939333
    [Abstract] [Full Text] [Related]

  • 6. Revealing covariance structures in fourier transform infrared and Raman microspectroscopy spectra: a study on pork muscle fiber tissue subjected to different processing parameters.
    Böcker U, Ofstad R, Wu Z, Bertram HC, Sockalingum GD, Manfait M, Egelandsdal B, Kohler A.
    Appl Spectrosc; 2007 Oct 06; 61(10):1032-9. PubMed ID: 17958951
    [Abstract] [Full Text] [Related]

  • 7. Effect of freezing temperature, thawing and cooking rate on water distribution in two pork qualities.
    Mortensen M, Andersen HJ, Engelsen SB, Bertram HC.
    Meat Sci; 2006 Jan 06; 72(1):34-42. PubMed ID: 22061371
    [Abstract] [Full Text] [Related]

  • 8. Development in myofibrillar water distribution of two pork qualities during 10-month freezer storage.
    Bertram HC, Andersen RH, Andersen HJ.
    Meat Sci; 2007 Jan 06; 75(1):128-33. PubMed ID: 22063420
    [Abstract] [Full Text] [Related]

  • 9. Extended multiplicative signal correction as a tool for separation and characterization of physical and chemical information in Fourier transform infrared microscopy images of cryo-sections of beef loin.
    Kohler A, Kirschner C, Oust A, Martens H.
    Appl Spectrosc; 2005 Jun 06; 59(6):707-16. PubMed ID: 16053536
    [Abstract] [Full Text] [Related]

  • 10. Changed dynamics in myofibrillar protein aggregation as a consequence of heating time and temperature.
    Promeyrat A, Bax ML, Traoré S, Aubry L, Santé-Lhoutellier V, Gatellier P.
    Meat Sci; 2010 Aug 06; 85(4):625-31. PubMed ID: 20416808
    [Abstract] [Full Text] [Related]

  • 11. Microscopic FT-IR/DSC system used to simultaneously investigate the conversion process of protein structure in porcine stratum corneum after pretreatment with skin penetration enhancers.
    Lin SY, Duan KJ, Lin TC.
    Methods Find Exp Clin Pharmacol; 1996 Apr 06; 18(3):175-81. PubMed ID: 8738068
    [Abstract] [Full Text] [Related]

  • 12. Water distribution and microstructure in enhanced pork.
    Bertram HC, Meyer RL, Wu Z, Zhou X, Andersen HJ.
    J Agric Food Chem; 2008 Aug 27; 56(16):7201-7. PubMed ID: 18642839
    [Abstract] [Full Text] [Related]

  • 13. Protein denaturation and water-protein interactions as affected by low temperature long time treatment of porcine longissimus dorsi.
    Christensen L, Bertram HC, Aaslyng MD, Christensen M.
    Meat Sci; 2011 Aug 27; 88(4):718-22. PubMed ID: 21450413
    [Abstract] [Full Text] [Related]

  • 14. Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier transform infrared spectroscopy.
    Murayama K, Tomida M.
    Biochemistry; 2004 Sep 14; 43(36):11526-32. PubMed ID: 15350138
    [Abstract] [Full Text] [Related]

  • 15. Monitoring secondary structural changes in salted and smoked salmon muscle myofiber proteins by FT-IR microspectroscopy.
    Carton I, Böcker U, Ofstad R, Sørheim O, Kohler A.
    J Agric Food Chem; 2009 May 13; 57(9):3563-70. PubMed ID: 19292444
    [Abstract] [Full Text] [Related]

  • 16. Multicomponent peak modeling of protein secondary structures: comparison of gaussian with lorentzian analytical methods for plant feed and seed molecular biology and chemistry research.
    Yu P.
    Appl Spectrosc; 2005 Nov 13; 59(11):1372-80. PubMed ID: 16316515
    [Abstract] [Full Text] [Related]

  • 17. Heating temperatures affect meat quality and vibrational spectroscopic properties of slow- and fast-growing chickens.
    Katemala S, Molee A, Thumanu K, Yongsawatdigul J.
    Poult Sci; 2023 Aug 13; 102(8):102754. PubMed ID: 37276701
    [Abstract] [Full Text] [Related]

  • 18. Structural study of the catalytic domain of PKCzeta using infrared spectroscopy and two-dimensional infrared correlation spectroscopy.
    Sánchez-Bautista S, Kazaks A, Beaulande M, Torrecillas A, Corbalán-García S, Gómez-Fernández JC.
    FEBS J; 2006 Jul 13; 273(14):3273-86. PubMed ID: 16792700
    [Abstract] [Full Text] [Related]

  • 19. Monitoring protein structural changes and hydration in bovine meat tissue due to salt substitutes by Fourier transform infrared (FTIR) microspectroscopy.
    Perisic N, Afseth NK, Ofstad R, Kohler A.
    J Agric Food Chem; 2011 Sep 28; 59(18):10052-61. PubMed ID: 21830764
    [Abstract] [Full Text] [Related]

  • 20. Hydration dependence of backbone and side chain polylysine dynamics: a 13C solid-state NMR and IR spectroscopy study.
    Krushelnitsky A, Faizullin D, Reichert D.
    Biopolymers; 2004 Jan 28; 73(1):1-15. PubMed ID: 14691935
    [Abstract] [Full Text] [Related]

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