메뉴 건너뛰기




Volumn 55, Issue 27, 2016, Pages 3794-3802

Determination of Protein Secondary Structure from Infrared Spectra Using Partial Least-Squares Regression

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; ARTIFICIAL INTELLIGENCE; DICHROISM; LEARNING SYSTEMS; LEAST SQUARES APPROXIMATIONS; MULTIVARIANT ANALYSIS; PROTEINS;

EID: 84978389793     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.6b00403     Document Type: Article
Times cited : (37)

References (39)
  • 1
    • 77955151599 scopus 로고    scopus 로고
    • Accurate determination of protein secondary structure content from Raman and Raman Optical Activity spectra
    • Kinalwa, M. N., Blanch, E. W., and Doig, A. J. (2010) Accurate determination of protein secondary structure content from Raman and Raman Optical Activity spectra Anal. Chem. 82, 6347-6349 10.1021/ac101334h
    • (2010) Anal. Chem. , vol.82 , pp. 6347-6349
    • Kinalwa, M.N.1    Blanch, E.W.2    Doig, A.J.3
  • 2
    • 33646196840 scopus 로고    scopus 로고
    • Evaluation of the information content in infrared spectra for protein secondary structure determination
    • Goormaghtigh, E., Ruysschaert, J. M., and Raussens, V. (2006) Evaluation of the information content in infrared spectra for protein secondary structure determination Biophys. J. 90, 2946-2957 10.1529/biophysj.105.072017
    • (2006) Biophys. J. , vol.90 , pp. 2946-2957
    • Goormaghtigh, E.1    Ruysschaert, J.M.2    Raussens, V.3
  • 3
    • 0030055763 scopus 로고    scopus 로고
    • A Fourier transform infrared spectroscopic study of P2 protein in reconstituted myelin
    • Stuart, B. H. (1996) A Fourier transform infrared spectroscopic study of P2 protein in reconstituted myelin IUBMB Life 39, 629-634 10.1080/15216549600201691
    • (1996) IUBMB Life , vol.39 , pp. 629-634
    • Stuart, B.H.1
  • 4
    • 0022463740 scopus 로고
    • Resolution-Enhanced Fourier-Transform Infrared-Spectroscopy of Enzymes
    • Susi, H. and Byler, D. M. (1986) Resolution-Enhanced Fourier-Transform Infrared-Spectroscopy of Enzymes Methods Enzymol. 130, 290-311 10.1016/0076-6879(86)30015-6
    • (1986) Methods Enzymol. , vol.130 , pp. 290-311
    • Susi, H.1    Byler, D.M.2
  • 5
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • Barth, A. (2007) Infrared spectroscopy of proteins Biochim. Biophys. Acta, Bioenerg. 1767, 1073-1101 10.1016/j.bbabio.2007.06.004
    • (2007) Biochim. Biophys. Acta, Bioenerg. , vol.1767 , pp. 1073-1101
    • Barth, A.1
  • 6
    • 27144468628 scopus 로고    scopus 로고
    • Use of infrared spectroscopy to monitor protein structure and stability
    • Manning, M. C. (2005) Use of infrared spectroscopy to monitor protein structure and stability Expert Rev. Proteomics 2, 731-743 10.1586/14789450.2.5.731
    • (2005) Expert Rev. Proteomics , vol.2 , pp. 731-743
    • Manning, M.C.1
  • 7
    • 0033584169 scopus 로고    scopus 로고
    • Identification of beta-turn and random coil amide III infrared bands for secondary structure estimation of proteins
    • Cai, S. W. and Singh, B. R. (1999) Identification of beta-turn and random coil amide III infrared bands for secondary structure estimation of proteins Biophys. Chem. 80, 7-20 10.1016/S0301-4622(99)00060-5
    • (1999) Biophys. Chem. , vol.80 , pp. 7-20
    • Cai, S.W.1    Singh, B.R.2
  • 8
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • Kong, J. and Yu, S. (2007) Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochim. Biophys. Sin. 39, 549-559 10.1111/j.1745-7270.2007.00320.x
    • (2007) Acta Biochim. Biophys. Sin. , vol.39 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 9
    • 0032818805 scopus 로고    scopus 로고
    • FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media
    • Haris, P. I. and Severcan, F. (1999) FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media J. Mol. Catal. B: Enzym. 7, 207-221 10.1016/S1381-1177(99)00030-2
    • (1999) J. Mol. Catal. B: Enzym. , vol.7 , pp. 207-221
    • Haris, P.I.1    Severcan, F.2
  • 11
    • 84893312751 scopus 로고    scopus 로고
    • Multi-spectroscopic analysis and molecular modeling on the interaction of curcumin and its derivatives with human serum albumin: A comparative study
    • Ge, Y.-S., Jin, C., Song, Z., Zhang, J.-Q., Jiang, F.-L., and Liu, Y. (2014) Multi-spectroscopic analysis and molecular modeling on the interaction of curcumin and its derivatives with human serum albumin: A comparative study Spectrochim. Acta, Part A 124, 265-276 10.1016/j.saa.2014.01.009
    • (2014) Spectrochim. Acta, Part A , vol.124 , pp. 265-276
    • Ge, Y.-S.1    Jin, C.2    Song, Z.3    Zhang, J.-Q.4    Jiang, F.-L.5    Liu, Y.6
  • 12
    • 0026349146 scopus 로고
    • Chemometrics, why, what and where to next?
    • Wold, S. (1991) Chemometrics, why, what and where to next? J. Pharm. Biomed. Anal. 9, 589-596 10.1016/0731-7085(91)80183-A
    • (1991) J. Pharm. Biomed. Anal. , vol.9 , pp. 589-596
    • Wold, S.1
  • 13
    • 50149102575 scopus 로고    scopus 로고
    • Determination of motor gasoline adulteration using FTIR spectroscopy and multivariate calibration
    • Al-Ghouti, M. A., Al-Degs, Y. S., and Amer, M. (2008) Determination of motor gasoline adulteration using FTIR spectroscopy and multivariate calibration Talanta 76, 1105-1112 10.1016/j.talanta.2008.05.024
    • (2008) Talanta , vol.76 , pp. 1105-1112
    • Al-Ghouti, M.A.1    Al-Degs, Y.S.2    Amer, M.3
  • 14
    • 84879450062 scopus 로고    scopus 로고
    • Determination of the myoglobin states in ground beef using non-invasive reflectance spectrometry and multivariate regression analysis
    • Bjelanovic, M., Sorheim, O., Slinde, E., Puolanne, E., Isaksson, T., and Egelandsdal, B. (2013) Determination of the myoglobin states in ground beef using non-invasive reflectance spectrometry and multivariate regression analysis Meat Sci. 95, 451-7 10.1016/j.meatsci.2013.05.021
    • (2013) Meat Sci. , vol.95 , pp. 451-457
    • Bjelanovic, M.1    Sorheim, O.2    Slinde, E.3    Puolanne, E.4    Isaksson, T.5    Egelandsdal, B.6
  • 15
    • 0035018354 scopus 로고    scopus 로고
    • Environmental features are important in determining protein secondary structure
    • Macdonald, J. R. and Johnson, W. C., Jr. (2001) Environmental features are important in determining protein secondary structure Protein Sci. 10, 1172-1177 10.1110/ps.420101
    • (2001) Protein Sci. , vol.10 , pp. 1172-1177
    • Macdonald, J.R.1    Johnson, W.C.2
  • 16
    • 49849104105 scopus 로고    scopus 로고
    • Reliability, repeatability and reproducibility: Analysis of measurement errors in continuous variables
    • Bartlett, J. W. and Frost, C. (2008) Reliability, repeatability and reproducibility: analysis of measurement errors in continuous variables Ultrasound in Obstetrics and Gynecology 31, 466-475 10.1002/uog.5256
    • (2008) Ultrasound in Obstetrics and Gynecology , vol.31 , pp. 466-475
    • Bartlett, J.W.1    Frost, C.2
  • 18
    • 77954876357 scopus 로고    scopus 로고
    • Genetic algorithm interval partial least squares regression combined successive projections algorithm for variable selection in near-infrared quantitative analysis of pigment in cucumber leaves
    • Zou, X., Zhao, J., Mao, H., Shi, J., Yin, X., and Li, Y. (2010) Genetic algorithm interval partial least squares regression combined successive projections algorithm for variable selection in near-infrared quantitative analysis of pigment in cucumber leaves Appl. Spectrosc. 64, 786-794 10.1366/000370210791666246
    • (2010) Appl. Spectrosc. , vol.64 , pp. 786-794
    • Zou, X.1    Zhao, J.2    Mao, H.3    Shi, J.4    Yin, X.5    Li, Y.6
  • 19
    • 11144304496 scopus 로고    scopus 로고
    • Application of the local regression method interval partial least-squares to the elucidation of protein secondary structure
    • Navea, S., Tauler, R., and de Juan, A. (2005) Application of the local regression method interval partial least-squares to the elucidation of protein secondary structure Anal. Biochem. 336, 231-242 10.1016/j.ab.2004.10.016
    • (2005) Anal. Biochem. , vol.336 , pp. 231-242
    • Navea, S.1    Tauler, R.2    De Juan, A.3
  • 20
    • 0004132705 scopus 로고
    • Martens, H. and Naes, T. (), Wiley, New York
    • Martens, H., and Naes, T. (1991) Multivariate Calibration, Wiley, New York.
    • (1991) Multivariate Calibration
  • 21
    • 54949141071 scopus 로고    scopus 로고
    • Determination of the secondary structure of proteins in different environments by FTIR-ATR spectroscopy and PLS regression
    • Wang, Y. Q., Boysen, R. I., Wood, B. R., Kansiz, M., McNaughton, D., and Hearn, M. T. W. (2008) Determination of the secondary structure of proteins in different environments by FTIR-ATR spectroscopy and PLS regression Biopolymers 89, 895-905 10.1002/bip.21022
    • (2008) Biopolymers , vol.89 , pp. 895-905
    • Wang, Y.Q.1    Boysen, R.I.2    Wood, B.R.3    Kansiz, M.4    McNaughton, D.5    Hearn, M.T.W.6
  • 22
    • 0034648775 scopus 로고    scopus 로고
    • Genetic algorithms applied to the selection of factors in principal component regression
    • Depczynski, U., Frost, V. J., and Molt, K. (2000) Genetic algorithms applied to the selection of factors in principal component regression Anal. Chim. Acta 420, 217-227 10.1016/S0003-2670(00)00893-X
    • (2000) Anal. Chim. Acta , vol.420 , pp. 217-227
    • Depczynski, U.1    Frost, V.J.2    Molt, K.3
  • 23
    • 0031101472 scopus 로고    scopus 로고
    • Multivariate classification of the infrared spectra of cell and tissue samples
    • Haaland, D. M., Jones, H. D. T., and Thomas, E. V. (1997) Multivariate classification of the infrared spectra of cell and tissue samples Appl. Spectrosc. 51, 340-345 10.1366/0003702971940468
    • (1997) Appl. Spectrosc. , vol.51 , pp. 340-345
    • Haaland, D.M.1    Jones, H.D.T.2    Thomas, E.V.3
  • 25
    • 0029774781 scopus 로고    scopus 로고
    • A Fourier transform infrared spectroscopic study of the secondary structure of myelin basic protein in reconstituted myelin
    • Stuart, B. H. (1996) A Fourier transform infrared spectroscopic study of the secondary structure of myelin basic protein in reconstituted myelin Biochemistry and molecular biology international 38, 839-845
    • (1996) Biochemistry and Molecular Biology International , vol.38 , pp. 839-845
    • Stuart, B.H.1
  • 26
    • 84889098193 scopus 로고    scopus 로고
    • Recent applications of ATR FTIR spectroscopy and imaging to proteins
    • Glassford, S. E., Byrne, B., and Kazarian, S. G. (2013) Recent applications of ATR FTIR spectroscopy and imaging to proteins Biochim. Biophys. Acta, Proteins Proteomics 1834, 2849-2858 10.1016/j.bbapap.2013.07.015
    • (2013) Biochim. Biophys. Acta, Proteins Proteomics , vol.1834 , pp. 2849-2858
    • Glassford, S.E.1    Byrne, B.2    Kazarian, S.G.3
  • 27
    • 84960925064 scopus 로고    scopus 로고
    • Attenuated Total Reflection Fourier Transform Infrared Spectroscopy
    • John Wiley & Sons, Ltd. Hoboken, New Jersey
    • Ramer, G. and Lendl, B. (2006) Attenuated Total Reflection Fourier Transform Infrared Spectroscopy. In Encyclopedia of Analytical Chemistry, John Wiley & Sons, Ltd., Hoboken, New Jersey.
    • (2006) Encyclopedia of Analytical Chemistry
    • Ramer, G.1    Lendl, B.2
  • 29
    • 0342679998 scopus 로고    scopus 로고
    • Transient non-native secondary structures during the refolding of α-lactalbumin detected by infrared spectroscopy
    • Forge, V., Troullier, A., Reinstädler, D., Dupont, Y., and Naumann, D. (2000) Transient non-native secondary structures during the refolding of α-lactalbumin detected by infrared spectroscopy Nat. Struct. Biol. 7, 78-86 10.1038/71286
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 78-86
    • Forge, V.1    Troullier, A.2    Reinstädler, D.3    Dupont, Y.4    Naumann, D.5
  • 30
    • 84894887900 scopus 로고
    • Computer Aided Design of Experiments
    • Kennard, R. W. and Stone, L. A. (1969) Computer Aided Design of Experiments Technometrics 11, 137-148 10.1080/00401706.1969.10490666
    • (1969) Technometrics , vol.11 , pp. 137-148
    • Kennard, R.W.1    Stone, L.A.2
  • 33
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22, 2577-2637 10.1002/bip.360221211
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 34
    • 0032801090 scopus 로고    scopus 로고
    • Estimating the uncertainty in estimates of root mean square error of prediction: Application to determining the size of an adequate test set in multivariate calibration
    • Faber, N. M. (1999) Estimating the uncertainty in estimates of root mean square error of prediction: application to determining the size of an adequate test set in multivariate calibration Chemom. Intell. Lab. Syst. 49, 79-89 10.1016/S0169-7439(99)00027-1
    • (1999) Chemom. Intell. Lab. Syst. , vol.49 , pp. 79-89
    • Faber, N.M.1
  • 35
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • Arrondo, J. L. R. and Goni, F. M. (1999) Structure and dynamics of membrane proteins as studied by infrared spectroscopy Prog. Biophys. Mol. Biol. 72, 367-405 10.1016/S0079-6107(99)00007-3
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 367-405
    • Arrondo, J.L.R.1    Goni, F.M.2
  • 36
    • 11144304496 scopus 로고    scopus 로고
    • Application of the local regression method interval partial least-squares to the elucidation of protein secondary structure
    • Navea, S., Tauler, R., and de Juan, A. (2005) Application of the local regression method interval partial least-squares to the elucidation of protein secondary structure Anal. Biochem. 336, 231-242 10.1016/j.ab.2004.10.016
    • (2005) Anal. Biochem. , vol.336 , pp. 231-242
    • Navea, S.1    Tauler, R.2    De Juan, A.3
  • 37
    • 0024997389 scopus 로고
    • Determination of the secondary structure-content of proteins in aqueous-solutions from their Amide-I and Amide-II infrared bands - Comparison between classical and partial least-sequares methods
    • Dousseau, F. and Pezolet, M. (1990) Determination of the secondary structure-content of proteins in aqueous-solutions from their Amide-I and Amide-II infrared bands-Comparison between classical and partial least-sequares methods Biochemistry 29, 8771-8779 10.1021/bi00489a038
    • (1990) Biochemistry , vol.29 , pp. 8771-8779
    • Dousseau, F.1    Pezolet, M.2
  • 38
    • 77954876357 scopus 로고    scopus 로고
    • Genetic Algorithm Interval Partial Least Squares Regression Combined Successive Projections Algorithm for Variable Selection in Near-Infrared Quantitative Analysis of Pigment in Cucumber Leaves
    • Zou, X. B., Zhao, J. W., Mao, H. P., Shi, J. Y., Yin, X. P., and Li, Y. X. (2010) Genetic Algorithm Interval Partial Least Squares Regression Combined Successive Projections Algorithm for Variable Selection in Near-Infrared Quantitative Analysis of Pigment in Cucumber Leaves Appl. Spectrosc. 64, 786-794 10.1366/000370210791666246
    • (2010) Appl. Spectrosc. , vol.64 , pp. 786-794
    • Zou, X.B.1    Zhao, J.W.2    Mao, H.P.3    Shi, J.Y.4    Yin, X.P.5    Li, Y.X.6
  • 39
    • 0033905297 scopus 로고    scopus 로고
    • Interval partial least-squares regression (iPLS): A comparative chemometric study with an example from near-infrared spectroscopy
    • Norgaard, L., Saudland, A., Wagner, J., Nielsen, J. P., Munck, L., and Engelsen, S. B. (2000) Interval partial least-squares regression (iPLS): A comparative chemometric study with an example from near-infrared spectroscopy Appl. Spectrosc. 54, 413-419 10.1366/0003702001949500
    • (2000) Appl. Spectrosc. , vol.54 , pp. 413-419
    • Norgaard, L.1    Saudland, A.2    Wagner, J.3    Nielsen, J.P.4    Munck, L.5    Engelsen, S.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.