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Year 2014, Volume: 27 Issue: 1, 637 - 644, 28.03.2014

Abstract

References

  • [1]. Chou and Fasman, G. D., “Prediction of the secondary structure of proteins from their amino acid sequence”, Adv. Enzymol, 47: 45-148 (1978).
  • [2]. Fasman, G.D., “Protein conformational prediction”, Trends Biochem. Sci., 14: 295-299 (1989).
  • [3]. Braun, W., “Distance geometry and related methods for protein structure determination from NMR data”, Quarterly Rev. Biophys., 19: 115- 157 (1987)
  • [4]. Wlodawer. A., Bott, R. and Sjoh, L., “The refined crystal structure of ribonuclease A at 2.0 A resolution”, J. Biol. Chem., 2S7: 1325-1332 (1982)
  • [5]. Pauling, L. and Corey, R. B., “Configurations of Polypeptide Chains With Favored Orientations Around Single Bonds: Two New Pleated Sheets”, Proc. Natl. Acad. Sci. USA, 37: 729-740 (1951).
  • [6]. Arrondo, J. L. R.; Muga, A.; Castresana, J., and God. F. M., “Quantitative studies of the structure of proteins in solution by fourier-transform infrared spectroscopy”, Prog. Biophys. Mol. Biol., 59: 23-56 (1993).
  • [7]. Susi, H. and Byler, D. M., “Resolution-enhanced Fourier transform infrared spectroscopy of enzymes”, Methods Enzymol., 130: 290-311 (1986).
  • [8]. Byler, D. M. and Susi, H., “Examination of the secondary structure of proteins by deconvolved FTIR spectra”, Biopolymers, 25: 469-487 (1986).
  • [9]. Surewicz, W. K. and Mantsch, H. H., Biochim. Biophys. Acta, 952: 115-130 (1988).
  • [10].Jackson, M.; Haris, P., and Chapman, D., “Fourier transform infrared spectroscopic studies of lipids, polypeptides and proteins”, J. Mol. Structure, 214: 329- 355 (1989).
  • [11].Jackson, M. and Mantsch, H. H., “The Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure”, Critical Reviews in Biochemistry and Molecular Biology, 30(2): 95-120 (1995).
  • [12].Elliot, A. and Ambrose. E. J., “Structure of Synthetic Polypeptides”, Nature, 165: 921-922 (1950).
  • [13].Ambrose, E. J. and Elliot, A., “Infra-Red Spectroscopic Studies of Globular Protein Structure”, Proc. R. Soc. London, Ser A, 208: 75-90 (1951).
  • [14].Susi, H.; Timasheff, S. N. and Stevens, L., “Infrared Spectra and Protein Conformations in Aqueous Solutions: I. The Amide I band in H2O and D2O Solutions”, J. Biol. Chem., 242: 5460- 5466 (1967).
  • [15].Timasheff, S. N.; Susi, H. and Stevens, L., “Infrared Spectra and Protein Conformations in Aqueous Solutions: II. Survey of Globular Proteins”, J. Biol. Chem., 242: 5467-5473 (1967).
  • [16].Levitt, M. and Chothia, C., “Structural patterns in globular proteins”, Nature, 261: 552–558 (1976).
  • [17].Orengo, C.A.; Michie, A.D.; Jones, S.; Jones, D.T.; MB Swindells, M.B., and JM Thornton, J.M., “CATH – a hierarchic classification of protein domain structures”, Structure, 5(8): 1093-1109 (1997).
  • [18].Ruegg, M.; Metzger, V. and Susi, H., “Computer analyses of characteristic infrared bands of globular proteins”, Biopolymers, 14: 1465-1471 (1975).
  • [19].Wang, J.; Sowa, M. G.; Ahmed M. K. and Mantsch, H. H., “Studies of photoionization dynamics of methylidyne, imidogen, and hydroxyl radicals at near-threshold photoelectron kinetic energies”, J. Phys. Chem., 98(2): 4748- 4755 (1994).
  • [20].Goormaghtigh, E.; Cabiaux Veronique and Ruysschaert, Jean-Marie, “Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films”, Eur. J. Biochem., 193(2): 409-420 (1990).
  • [21].Levitt, M. and Greer, J., “Automatic identification of secondary structure in globular proteins”, J. Mol. Biol., 114: 181-239 (1977).
  • [22].Kong Jilie and Yu Shaoning, “Fourier Transform Infrared Spectroscopic Analysis of Protein Secondary Structures”, Acta Biochimica et Biophysica Sinica, 39(8): 549–559 (2007).
  • [23].Krimm, S. and Bandekar, J., “Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins”, Adv. Proteins Chem., 38: 181-364 (1986).
  • [24].Banker, J., “Amide Modes and Protein Confimation”, Biochim. Biophys. Acta, 1120: 123-143 (1992).
  • [25].Koenig, J.K. and Tabb, D.L., Analytical Application of FT-IR to Molecular and Biological Systems. D. Reidel: Boston 1980 [26].Dong, A.; Huang, P. and Caughey, W.S., “Protein secondary structures in water from second-derivative amide I infrared spectra”, Biochemistry, 29: 3303−3308 (1990).
  • [27].Lee, D.C.; Haris, P.I.; Chapman, D. and Mitchell, R.C., “Determination of protein secondary structure using factor analysis of infrared spectra”, Biochemistry, 29: 9185−9193 (1990).

Evaluation of the Protein Secondary Structures Using Fourier Transform Infrared Spectroscopy

Year 2014, Volume: 27 Issue: 1, 637 - 644, 28.03.2014

Abstract

Fourier transform infrared (FTIR) spectroscopy is an attractive tool for proteomics research as it can be used to rapidly characterize protein secondary structure in aqueous solution. Fourier transform infrared spectrometry is well known as a powerful tool for determination of secondary structures of proteins. This paper presents the most recent experimental results obtained in our laboratory for this kind of analysis. A PeakFit operation was performed and some observations were made.

References

  • [1]. Chou and Fasman, G. D., “Prediction of the secondary structure of proteins from their amino acid sequence”, Adv. Enzymol, 47: 45-148 (1978).
  • [2]. Fasman, G.D., “Protein conformational prediction”, Trends Biochem. Sci., 14: 295-299 (1989).
  • [3]. Braun, W., “Distance geometry and related methods for protein structure determination from NMR data”, Quarterly Rev. Biophys., 19: 115- 157 (1987)
  • [4]. Wlodawer. A., Bott, R. and Sjoh, L., “The refined crystal structure of ribonuclease A at 2.0 A resolution”, J. Biol. Chem., 2S7: 1325-1332 (1982)
  • [5]. Pauling, L. and Corey, R. B., “Configurations of Polypeptide Chains With Favored Orientations Around Single Bonds: Two New Pleated Sheets”, Proc. Natl. Acad. Sci. USA, 37: 729-740 (1951).
  • [6]. Arrondo, J. L. R.; Muga, A.; Castresana, J., and God. F. M., “Quantitative studies of the structure of proteins in solution by fourier-transform infrared spectroscopy”, Prog. Biophys. Mol. Biol., 59: 23-56 (1993).
  • [7]. Susi, H. and Byler, D. M., “Resolution-enhanced Fourier transform infrared spectroscopy of enzymes”, Methods Enzymol., 130: 290-311 (1986).
  • [8]. Byler, D. M. and Susi, H., “Examination of the secondary structure of proteins by deconvolved FTIR spectra”, Biopolymers, 25: 469-487 (1986).
  • [9]. Surewicz, W. K. and Mantsch, H. H., Biochim. Biophys. Acta, 952: 115-130 (1988).
  • [10].Jackson, M.; Haris, P., and Chapman, D., “Fourier transform infrared spectroscopic studies of lipids, polypeptides and proteins”, J. Mol. Structure, 214: 329- 355 (1989).
  • [11].Jackson, M. and Mantsch, H. H., “The Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure”, Critical Reviews in Biochemistry and Molecular Biology, 30(2): 95-120 (1995).
  • [12].Elliot, A. and Ambrose. E. J., “Structure of Synthetic Polypeptides”, Nature, 165: 921-922 (1950).
  • [13].Ambrose, E. J. and Elliot, A., “Infra-Red Spectroscopic Studies of Globular Protein Structure”, Proc. R. Soc. London, Ser A, 208: 75-90 (1951).
  • [14].Susi, H.; Timasheff, S. N. and Stevens, L., “Infrared Spectra and Protein Conformations in Aqueous Solutions: I. The Amide I band in H2O and D2O Solutions”, J. Biol. Chem., 242: 5460- 5466 (1967).
  • [15].Timasheff, S. N.; Susi, H. and Stevens, L., “Infrared Spectra and Protein Conformations in Aqueous Solutions: II. Survey of Globular Proteins”, J. Biol. Chem., 242: 5467-5473 (1967).
  • [16].Levitt, M. and Chothia, C., “Structural patterns in globular proteins”, Nature, 261: 552–558 (1976).
  • [17].Orengo, C.A.; Michie, A.D.; Jones, S.; Jones, D.T.; MB Swindells, M.B., and JM Thornton, J.M., “CATH – a hierarchic classification of protein domain structures”, Structure, 5(8): 1093-1109 (1997).
  • [18].Ruegg, M.; Metzger, V. and Susi, H., “Computer analyses of characteristic infrared bands of globular proteins”, Biopolymers, 14: 1465-1471 (1975).
  • [19].Wang, J.; Sowa, M. G.; Ahmed M. K. and Mantsch, H. H., “Studies of photoionization dynamics of methylidyne, imidogen, and hydroxyl radicals at near-threshold photoelectron kinetic energies”, J. Phys. Chem., 98(2): 4748- 4755 (1994).
  • [20].Goormaghtigh, E.; Cabiaux Veronique and Ruysschaert, Jean-Marie, “Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films”, Eur. J. Biochem., 193(2): 409-420 (1990).
  • [21].Levitt, M. and Greer, J., “Automatic identification of secondary structure in globular proteins”, J. Mol. Biol., 114: 181-239 (1977).
  • [22].Kong Jilie and Yu Shaoning, “Fourier Transform Infrared Spectroscopic Analysis of Protein Secondary Structures”, Acta Biochimica et Biophysica Sinica, 39(8): 549–559 (2007).
  • [23].Krimm, S. and Bandekar, J., “Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins”, Adv. Proteins Chem., 38: 181-364 (1986).
  • [24].Banker, J., “Amide Modes and Protein Confimation”, Biochim. Biophys. Acta, 1120: 123-143 (1992).
  • [25].Koenig, J.K. and Tabb, D.L., Analytical Application of FT-IR to Molecular and Biological Systems. D. Reidel: Boston 1980 [26].Dong, A.; Huang, P. and Caughey, W.S., “Protein secondary structures in water from second-derivative amide I infrared spectra”, Biochemistry, 29: 3303−3308 (1990).
  • [27].Lee, D.C.; Haris, P.I.; Chapman, D. and Mitchell, R.C., “Determination of protein secondary structure using factor analysis of infrared spectra”, Biochemistry, 29: 9185−9193 (1990).
There are 26 citations in total.

Details

Primary Language English
Subjects Engineering
Journal Section Chemistry
Authors

Y Aboul-eneın

Andrei Bunacıu This is me

Serban Fleschın This is me

Publication Date March 28, 2014
Published in Issue Year 2014 Volume: 27 Issue: 1

Cite

APA Aboul-eneın, Y., Bunacıu, A., & Fleschın, S. (2014). Evaluation of the Protein Secondary Structures Using Fourier Transform Infrared Spectroscopy. Gazi University Journal of Science, 27(1), 637-644.
AMA Aboul-eneın Y, Bunacıu A, Fleschın S. Evaluation of the Protein Secondary Structures Using Fourier Transform Infrared Spectroscopy. Gazi University Journal of Science. March 2014;27(1):637-644.
Chicago Aboul-eneın, Y, Andrei Bunacıu, and Serban Fleschın. “Evaluation of the Protein Secondary Structures Using Fourier Transform Infrared Spectroscopy”. Gazi University Journal of Science 27, no. 1 (March 2014): 637-44.
EndNote Aboul-eneın Y, Bunacıu A, Fleschın S (March 1, 2014) Evaluation of the Protein Secondary Structures Using Fourier Transform Infrared Spectroscopy. Gazi University Journal of Science 27 1 637–644.
IEEE Y. Aboul-eneın, A. Bunacıu, and S. Fleschın, “Evaluation of the Protein Secondary Structures Using Fourier Transform Infrared Spectroscopy”, Gazi University Journal of Science, vol. 27, no. 1, pp. 637–644, 2014.
ISNAD Aboul-eneın, Y et al. “Evaluation of the Protein Secondary Structures Using Fourier Transform Infrared Spectroscopy”. Gazi University Journal of Science 27/1 (March 2014), 637-644.
JAMA Aboul-eneın Y, Bunacıu A, Fleschın S. Evaluation of the Protein Secondary Structures Using Fourier Transform Infrared Spectroscopy. Gazi University Journal of Science. 2014;27:637–644.
MLA Aboul-eneın, Y et al. “Evaluation of the Protein Secondary Structures Using Fourier Transform Infrared Spectroscopy”. Gazi University Journal of Science, vol. 27, no. 1, 2014, pp. 637-44.
Vancouver Aboul-eneın Y, Bunacıu A, Fleschın S. Evaluation of the Protein Secondary Structures Using Fourier Transform Infrared Spectroscopy. Gazi University Journal of Science. 2014;27(1):637-44.