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240 related items for PubMed ID: 15214810

  • 1. A new approach for determining the stability of recombinant human epidermal growth factor by thermal Fourier transform infrared (FTIR) microspectroscopy.
    Yang CH, Wu PC, Huang YB, Tsai YH.
    J Biomol Struct Dyn; 2004 Aug; 22(1):101-10. PubMed ID: 15214810
    [Abstract] [Full Text] [Related]

  • 2. Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by Fourier transform infrared spectroscopy and differential scanning calorimetry.
    Choi SM, Ma CY.
    J Agric Food Chem; 2005 Oct 05; 53(20):8046-53. PubMed ID: 16190669
    [Abstract] [Full Text] [Related]

  • 3. Conformational study of globulin from rice (Oryza sativa) seeds by Fourier-transform infrared spectroscopy.
    Ellepola SW, Choi SM, Ma CY.
    Int J Biol Macromol; 2005 Oct 30; 37(1-2):12-20. PubMed ID: 16140371
    [Abstract] [Full Text] [Related]

  • 4. Study of oat globulin conformation by Fourier transform infrared spectroscopy.
    Ma CY, Rout MK, Mock WY.
    J Agric Food Chem; 2001 Jul 30; 49(7):3328-34. PubMed ID: 11453771
    [Abstract] [Full Text] [Related]

  • 5. Fourier-transform infrared spectroscopic study of globulin from Phaseolus angularis (red bean).
    Meng GT, Ma CY.
    Int J Biol Macromol; 2001 Dec 10; 29(4-5):287-94. PubMed ID: 11718826
    [Abstract] [Full Text] [Related]

  • 6. Fundamental analysis of recombinant human epidermal growth factor in solution with biophysical methods.
    Kim NA, Lim DG, Lim JY, Kim KH, Jeong SH.
    Drug Dev Ind Pharm; 2015 Feb 10; 41(2):300-6. PubMed ID: 24502269
    [Abstract] [Full Text] [Related]

  • 7. Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution.
    Dong A, Kendrick B, Kreilgârd L, Matsuura J, Manning MC, Carpenter JF.
    Arch Biochem Biophys; 1997 Nov 15; 347(2):213-20. PubMed ID: 9367527
    [Abstract] [Full Text] [Related]

  • 8. pH- and thermal-dependent conformational transition of PGAIPG, a repeated hexapeptide sequence from tropoelastin.
    Lin SY, Hsieh TF, Wei YS.
    Peptides; 2005 Apr 15; 26(4):543-9. PubMed ID: 15752567
    [Abstract] [Full Text] [Related]

  • 9. Secondary structure and temperature-induced unfolding and refolding of ribonuclease T1 in aqueous solution. A Fourier transform infrared spectroscopic study.
    Fabian H, Schultz C, Naumann D, Landt O, Hahn U, Saenger W.
    J Mol Biol; 1993 Aug 05; 232(3):967-81. PubMed ID: 8355280
    [Abstract] [Full Text] [Related]

  • 10. Changes in protein conformation and dynamics upon complex formation of brain-derived neurotrophic factor and its receptor: investigation by isotope-edited Fourier transform IR spectroscopy.
    Li T, Talvenheimo J, Zeni L, Rosenfeld R, Stearns G, Arakawa T.
    Biopolymers; 2002 Aug 05; 67(1):10-9. PubMed ID: 11842409
    [Abstract] [Full Text] [Related]

  • 11. Calcium-dependent conformational change and thermal stability of the isolated PsbO protein detected by FTIR spectroscopy.
    Heredia P, De Las Rivas J.
    Biochemistry; 2003 Oct 14; 42(40):11831-8. PubMed ID: 14529295
    [Abstract] [Full Text] [Related]

  • 12. Combined effect of heat treatment and ionic strength on the functionality of whey proteins.
    Hussain R, Gaiani C, Jeandel C, Ghanbaja J, Scher J.
    J Dairy Sci; 2012 Nov 14; 95(11):6260-73. PubMed ID: 22939789
    [Abstract] [Full Text] [Related]

  • 13. Thermal-induced changes in the secondary conformation of superoxide dismutase containing different metal ions.
    Chang CH, Lin SY, Tsai YH.
    J Biomol Struct Dyn; 2002 Aug 14; 20(1):81-6. PubMed ID: 12144354
    [Abstract] [Full Text] [Related]

  • 14. Pressure- and temperature-induced unfolding and aggregation of recombinant human interferon-gamma: a Fourier transform infrared spectroscopy study.
    Goossens K, Haelewyn J, Meersman F, De Ley M, Heremans K.
    Biochem J; 2003 Mar 01; 370(Pt 2):529-35. PubMed ID: 12425720
    [Abstract] [Full Text] [Related]

  • 15. FTIR studies of recombinant human granulocyte-macrophage colony-stimulating factor in aqueous solutions: secondary structure, disulfide reduction and thermal behavior.
    Jiang H, Song Z, Ling M, Yang S, Du Z.
    Biochim Biophys Acta; 1996 May 23; 1294(2):121-8. PubMed ID: 8645729
    [Abstract] [Full Text] [Related]

  • 16. Implementation of an FTIR calibration curve for fast and objective determination of changes in protein secondary structure during formulation development.
    Vonhoff S, Condliffe J, Schiffter H.
    J Pharm Biomed Anal; 2010 Jan 05; 51(1):39-45. PubMed ID: 19726151
    [Abstract] [Full Text] [Related]

  • 17. Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering.
    Panick G, Malessa R, Winter R.
    Biochemistry; 1999 May 18; 38(20):6512-9. PubMed ID: 10350469
    [Abstract] [Full Text] [Related]

  • 18. Pressure-induced transformation of alpha-helix to beta-sheet in the secondary structures of amyloid beta (1-40) peptide exacerbated by temperature.
    Lin SY, Chu HL, Wei YS.
    J Biomol Struct Dyn; 2002 Feb 18; 19(4):619-25. PubMed ID: 11843623
    [Abstract] [Full Text] [Related]

  • 19. [Study on thermal unfolding process of trichosanthin by FTIR spectroscopy].
    Bian W, Sun S, Wong RN, Zhou Q, Hu X.
    Guang Pu Xue Yu Guang Pu Fen Xi; 2000 Aug 18; 20(4):471-3. PubMed ID: 12945351
    [Abstract] [Full Text] [Related]

  • 20. FTIR study of the thermal denaturation of horseradish and cytochrome c peroxidases in D2O.
    Holzbaur IE, English AM, Ismail AA.
    Biochemistry; 1996 Apr 30; 35(17):5488-94. PubMed ID: 8611540
    [Abstract] [Full Text] [Related]

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