메뉴 건너뛰기




Volumn 1844, Issue 3, 2014, Pages 593-606

The transition from the native to the acid-state characterized by multi-spectroscopy approach: Study for the holo-form of bovine α-lactalbumin

Author keywords

A state molten globule; Holo lactalbumin; Multi spectral analysis; Principal component analysis; Protein structure; Two dimensional correlation spectroscopy

Indexed keywords

ALPHA LACTALBUMIN; CARBOXYL GROUP;

EID: 84893358278     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.12.018     Document Type: Article
Times cited : (22)

References (67)
  • 1
    • 0031050429 scopus 로고    scopus 로고
    • Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering
    • M. Kataoka, F. Tokunaga, K. Kuwajima, and Y. Goto Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering Protein Sci. 6 1997 422 430 (Pubitemid 27079935)
    • (1997) Protein Science , vol.6 , Issue.2 , pp. 422-430
    • Kataoka, M.1    Kuwajima, K.2    Tokunaga, F.3    Goto, Y.4
  • 3
    • 0034711229 scopus 로고    scopus 로고
    • Crystal structures of Apo- and holo-bovine α-lactalbumin at 2.2-Å resolution reveal an effect of calcium on inter-lobe interactions
    • DOI 10.1074/jbc.M004752200
    • E.D. Chrysina, K. Brew, and K.R. Acharya Crystal structures of apo- and holo-bovine α-lactalbumin at 2.2-Å resolution reveal an effect of calcium on inter-lobe interactions J. Biol. Chem. 275 2000 37021 37029 (Pubitemid 32002118)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.47 , pp. 37021-37029
    • Chrysina, E.D.1    Brew, K.2    Acharya, K.R.3
  • 4
    • 0035970302 scopus 로고    scopus 로고
    • Comparison of the structural and dynamical properties of holo and apo bovine α-lactalbumin by NMR spectroscopy
    • DOI 10.1006/jmbi.2001.4530
    • R. Wijesinha-Bettoni, C.M. Dobson, and C. Redfield Comparison of the structural and dynamical properties of holo and apo bovine α-lactalbumin by NMR spectroscopy J. Mol. Biol. 307 2001 885 898 (Pubitemid 33027666)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.3 , pp. 885-898
    • Wijesinha-Bettoni, R.1    Dobson, C.M.2    Redfield, C.3
  • 5
    • 0342679998 scopus 로고    scopus 로고
    • Transient non-native secondary structures during the refolding of α- lactalbumin detected by infrared spectroscopy
    • DOI 10.1038/71286
    • A. Troullier, D. Reinstädler, Y. Dupont, D. Naumann, and V. Forge Transient non-native secondary structures during the refolding of α-lactalbumin detected by infrared spectroscopy Nat. Struct. Biol. 7 2000 78 86 (Pubitemid 30043253)
    • (2000) Nature Structural Biology , vol.7 , Issue.1 , pp. 78-86
    • Troullier, A.1    Reinstadler, D.2    Dupont, Y.3    Naumann, D.4    Forge, V.5
  • 6
    • 0031811980 scopus 로고    scopus 로고
    • Remarkable destabilization of recombinant α-lactalbumin by an extraneous N-terminal methionyl residue
    • N. Ishikawa, T. Chiba, L.T. Chen, A. Shimizu, M. Ikeguchi, and S. Sugai Remarkable destabilization of recombinant alpha-lactalbumin by an extraneous N-terminal methionyl residue Protein Eng. 11 1998 333 335 (Pubitemid 28279655)
    • (1998) Protein Engineering , vol.11 , Issue.5 , pp. 333-335
    • Ishikawa, N.1    Chiba, T.2    Chen, L.T.3    Shimizu, A.4    Ikeguchi, M.5    Sugai, S.6
  • 7
    • 0026516468 scopus 로고
    • Proteolytic digestion of α-lactalbumin: Physiological implications
    • Y. Hirai, E.A. Permyakov, and L.J. Berliner Proteolytic digestion of α-lactalbumin: physiological implications J. Protein Chem. 11 1992 51 57
    • (1992) J. Protein Chem. , vol.11 , pp. 51-57
    • Hirai, Y.1    Permyakov, E.A.2    Berliner, L.J.3
  • 9
  • 10
    • 80051604144 scopus 로고    scopus 로고
    • Bioactivity of α-lactalbumin related to its interaction with fatty acids: A review
    • C. Barbana, L. Sánchez, and M.D. Pérez Bioactivity of α-lactalbumin related to its interaction with fatty acids: a review Crit. Rev. Food Sci. Nutr. 51 2011 783 794
    • (2011) Crit. Rev. Food Sci. Nutr. , vol.51 , pp. 783-794
    • Barbana, C.1    Sánchez, L.2    Pérez, M.D.3
  • 11
    • 78049232312 scopus 로고    scopus 로고
    • Structure and function of human α-lactalbumin made lethal to tumor cells (HAMLET)-type complexes
    • A.-K. Mossberg, K.H. Mok, L.A. Morozova-Roche, and C. Svanborg Structure and function of human α-lactalbumin made lethal to tumor cells (HAMLET)-type complexes FEBS J. 277 2010 4614 4625
    • (2010) FEBS J. , vol.277 , pp. 4614-4625
    • Mossberg, A.-K.1    Mok, K.H.2    Morozova-Roche, L.A.3    Svanborg, C.4
  • 12
    • 0023626273 scopus 로고
    • Protein folding: Hypotheses and experiments
    • O.B. Ptitsyn Protein folding: hypotheses and experiments J. Protein Chem. 6 1987 273 293 (Pubitemid 17139497)
    • (1987) Journal of Protein Chemistry , vol.6 , Issue.4 , pp. 273-293
    • Ptitsyn, O.B.1
  • 13
    • 1842464687 scopus 로고    scopus 로고
    • Inter-residue interactions in protein folding and stability
    • DOI 10.1016/j.pbiomolbio.2003.09.003, PII S0079610703000816
    • M.M. Gromiha, and S. Selvaraj Inter-residue interactions in protein folding and stability Prog. Biophys. Mol. Biol. 86 2004 235 277 (Pubitemid 39027234)
    • (2004) Progress in Biophysics and Molecular Biology , vol.86 , Issue.2 , pp. 235-277
    • Gromiha, M.M.1    Selvaraj, S.2
  • 14
    • 38949161177 scopus 로고    scopus 로고
    • Surface properties are highly sensitive to small pH induced changes in the 3-D structure of α-lactalbumin
    • DOI 10.1021/bi700999r
    • C. Gao, R. Wijesinha-Bettoni, P.J. Wilde, E.N.C. Mills, L.J. Smith, and A.R. Mackie Surface properties are highly sensitive to small pH induced changes in the 3-D structure of α-lactalbumin Biochemistry 47 2008 1659 1666 (Pubitemid 351231215)
    • (2008) Biochemistry , vol.47 , Issue.6 , pp. 1659-1666
    • Gao, C.1    Wijesinha-Bettoni, R.2    Wilde, P.J.3    Mills, E.N.C.4    Smith, L.J.5    Mackie, A.R.6
  • 15
    • 0037110569 scopus 로고    scopus 로고
    • Molten globule of bovine α-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: A comparative analysis by circular dichroism spectroscopy and limited proteolysis
    • DOI 10.1002/prot.10234
    • P. Polverino de Laureto, E. Frare, R. Gottardo, and A. Fontana Molten globule of bovine α-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: a comparative analysis by circular dichroism spectroscopy and limited proteolysis Proteins Struct. Funct. Genet. 49 2002 385 397 (Pubitemid 35231474)
    • (2002) Proteins: Structure, Function and Genetics , vol.49 , Issue.3 , pp. 385-397
    • De Laureto, P.P.1    Frare, E.2    Gottardo, R.3    Fontana, A.4
  • 17
    • 0031963564 scopus 로고    scopus 로고
    • Is the molten globule a third thermodynamic state of protein? The example of α-lactalbumin
    • DOI 10.1002/(SICI)1097-0134(19980101)30:1<43::AID-PROT4>3.0.CO;2-L
    • W. Pfeil Is the molten globule a third thermodynamic state of protein? The example of α-lactalbumin Proteins Struct. Funct. Bioinforma. 30 1998 43 48 (Pubitemid 28036109)
    • (1998) Proteins: Structure, Function and Genetics , vol.30 , Issue.1 , pp. 43-48
    • Pfeil, W.1
  • 18
    • 0034646563 scopus 로고    scopus 로고
    • Energetic basis of structural stability in the molten globule state: α-lactalbumin
    • Y.V. Griko Energetic basis of structural stability in the molten globule state: α-lactalbumin J. Mol. Biol. 297 2000 1259 1268
    • (2000) J. Mol. Biol. , vol.297 , pp. 1259-1268
    • Griko, Y.V.1
  • 19
    • 0035823118 scopus 로고    scopus 로고
    • Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules
    • DOI 10.1006/jmbi.2001.4927
    • R. Wijesinha-Bettoni, C.M. Dobson, and C. Redfield Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules J. Mol. Biol. 312 2001 261 273 (Pubitemid 32835691)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.1 , pp. 261-273
    • Wijesinha-Bettoni, R.1    Dobson, C.M.2    Redfield, C.3
  • 20
    • 0029585995 scopus 로고
    • Vibrational Raman optical activity of α-lactalbumin: Comparison with lysozyme, and evidence for native tertiary folds in molten globule states
    • DOI 10.1006/jmbi.1995.0652
    • G. Wilson, S.J. Ford, A. Cooper, L. Hecht, Z.Q. Wen, and L.D. Barron Vibrational Raman optical activity of α-lactalbumin: comparison with lysozyme, and evidence for native tertiary folds in molten globule states J. Mol. Biol. 254 1995 747 760 (Pubitemid 26001805)
    • (1995) Journal of Molecular Biology , vol.254 , Issue.4 , pp. 747-760
    • Wilson, G.1    Ford, S.J.2    Cooper, A.3    Hecht, L.4    Wen, Z.Q.5    Barron, L.D.6
  • 21
    • 70350524972 scopus 로고    scopus 로고
    • The human α-lactalbumin molten globule: Comparison of structural preferences at pH 2 and pH 7
    • H.I. Rösner, and C. Redfield The human α-lactalbumin molten globule: comparison of structural preferences at pH 2 and pH 7 J. Mol. Biol. 394 2009 351 362
    • (2009) J. Mol. Biol. , vol.394 , pp. 351-362
    • Rösner, H.I.1    Redfield, C.2
  • 22
    • 0345828173 scopus 로고    scopus 로고
    • How many molten globules states exist?
    • V.N. Uverskii How many molten globules states exist? Biofizika 43 1998 416 421
    • (1998) Biofizika , vol.43 , pp. 416-421
    • Uverskii, V.N.1
  • 23
    • 77957970492 scopus 로고    scopus 로고
    • Dry molten globule intermediates and the mechanism of protein unfolding
    • R.L. Baldwin, C. Frieden, and G.D. Rose Dry molten globule intermediates and the mechanism of protein unfolding Proteins Struct. Funct. Bioinforma. 78 2010 2725 2737
    • (2010) Proteins Struct. Funct. Bioinforma. , vol.78 , pp. 2725-2737
    • Baldwin, R.L.1    Frieden, C.2    Rose, G.D.3
  • 24
    • 69249222742 scopus 로고    scopus 로고
    • Protein secondary structure content in solution, films and tissues: Redundancy and complementarity of the information content in circular dichroism, transmission and ATR FTIR spectra
    • E. Goormaghtigh, R. Gasper, A. Bénard, A. Goldsztein, and V. Raussens Protein secondary structure content in solution, films and tissues: redundancy and complementarity of the information content in circular dichroism, transmission and ATR FTIR spectra Biochim. Biophys. Acta 1794 2009 1332 1343
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1332-1343
    • Goormaghtigh, E.1    Gasper, R.2    Bénard, A.3    Goldsztein, A.4    Raussens, V.5
  • 25
    • 33646416198 scopus 로고    scopus 로고
    • Two-dimensional correlation analysis of Raman optical activity data on the α-helix-to-β-sheet transition in poly(l-lysine)
    • L. Ashton, L.D. Barron, B. Czarnik-Matusewicz, L. Hecht, J. Hyde, and E.W. Blanch Two-dimensional correlation analysis of Raman optical activity data on the α-helix-to-β-sheet transition in poly(l-lysine) Mol. Phys. 104 2006 1429 1445
    • (2006) Mol. Phys. , vol.104 , pp. 1429-1445
    • Ashton, L.1    Barron, L.D.2    Czarnik-Matusewicz, B.3    Hecht, L.4    Hyde, J.5    Blanch, E.W.6
  • 26
    • 77954219546 scopus 로고    scopus 로고
    • PH-induced conformational transitions in α-lactalbumin investigated with two-dimensional Raman correlation variance plots and moving windows
    • L. Ashton, and E.W. Blanch pH-induced conformational transitions in α-lactalbumin investigated with two-dimensional Raman correlation variance plots and moving windows J. Mol. Struct. 974 2010 132 138
    • (2010) J. Mol. Struct. , vol.974 , pp. 132-138
    • Ashton, L.1    Blanch, E.W.2
  • 27
    • 61949248655 scopus 로고    scopus 로고
    • A study of urea-dependent denaturation of β-lactoglobulin by principal component analysis and two-dimensional correlation spectroscopy
    • B. Czarnik-Matusewicz, S.B. Kim, and Y.M. Jung A study of urea-dependent denaturation of β-lactoglobulin by principal component analysis and two-dimensional correlation spectroscopy J. Phys. Chem. B 113 2009 559 566
    • (2009) J. Phys. Chem. B , vol.113 , pp. 559-566
    • Czarnik-Matusewicz, B.1    Kim, S.B.2    Jung, Y.M.3
  • 29
    • 78449267576 scopus 로고    scopus 로고
    • Collision cross sections of proteins and their complexes: A calibration framework and database for gas-phase structural biology
    • M.F. Bush, Z. Hall, K. Giles, J. Hoyes, C.V. Robinson, and B.T. Ruotolo Collision cross sections of proteins and their complexes: a calibration framework and database for gas-phase structural biology Anal. Chem. 82 2010 9557 9565
    • (2010) Anal. Chem. , vol.82 , pp. 9557-9565
    • Bush, M.F.1    Hall, Z.2    Giles, K.3    Hoyes, J.4    Robinson, C.V.5    Ruotolo, B.T.6
  • 30
    • 84861098652 scopus 로고    scopus 로고
    • Analysis of the molten globule state of bovine α-lactalbumin by using vibrational circular dichroism
    • S.R. Ryu, B. Czarnik-Matusewicz, R.K. Dukor, L.A. Nafie, and Y.M. Jung Analysis of the molten globule state of bovine α-lactalbumin by using vibrational circular dichroism Vib. Spectrosc. 60 2012 68 72
    • (2012) Vib. Spectrosc. , vol.60 , pp. 68-72
    • Ryu, S.R.1    Czarnik-Matusewicz, B.2    Dukor, R.K.3    Nafie, L.A.4    Jung, Y.M.5
  • 31
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326 (Pubitemid 19277112)
    • (1989) Analytical Biochemistry , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 33
    • 0024622619 scopus 로고
    • On the spectral subtraction of water from the FT-IR spectra of aqueous solutions of proteins
    • F. Dousseau, M. Therrien, and M. Pézolet On the spectral subtraction of water from the FT-IR spectra of aqueous solutions of proteins Appl. Spectrosc. 43 1989 538 542
    • (1989) Appl. Spectrosc. , vol.43 , pp. 538-542
    • Dousseau, F.1    Therrien, M.2    Pézolet, M.3
  • 34
    • 44749094727 scopus 로고    scopus 로고
    • Scaling techniques to enhance two-dimensional correlation spectra
    • I. Noda Scaling techniques to enhance two-dimensional correlation spectra J. Mol. Struct. 883-884 2008 216 227
    • (2008) J. Mol. Struct. , vol.883-884 , pp. 216-227
    • Noda, I.1
  • 35
    • 80052314121 scopus 로고    scopus 로고
    • Charge-surface correlation in electrospray ionization of folded and unfolded proteins
    • L. Testa, S. Brocca, and R. Grandori Charge-surface correlation in electrospray ionization of folded and unfolded proteins Anal. Chem. 83 2011 6459 6463
    • (2011) Anal. Chem. , vol.83 , pp. 6459-6463
    • Testa, L.1    Brocca, S.2    Grandori, R.3
  • 37
    • 84873042766 scopus 로고    scopus 로고
    • Probing conformational changes of ubiquitin by host-guest chemistry using electrospray ionization mass spectrometry
    • J.W. Lee, S.W. Heo, S.J. Lee, J.Y. Ko, H. Kim, and H.I. Kim Probing conformational changes of ubiquitin by host-guest chemistry using electrospray ionization mass spectrometry J. Am. Soc. Mass Spectrom. 24 2013 21 29
    • (2013) J. Am. Soc. Mass Spectrom. , vol.24 , pp. 21-29
    • Lee, J.W.1    Heo, S.W.2    Lee, S.J.3    Ko, J.Y.4    Kim, H.5    Kim, H.I.6
  • 38
    • 80054892557 scopus 로고    scopus 로고
    • Structural stability from solution to the gas phase: Native solution structure of ubiquitin survives analysis in a solvent-free ion mobility-mass spectrometry environment
    • T. Wyttenbach, and M.T. Bowers Structural stability from solution to the gas phase: native solution structure of ubiquitin survives analysis in a solvent-free ion mobility-mass spectrometry environment J. Phys. Chem. B 115 2011 12266 12275
    • (2011) J. Phys. Chem. B , vol.115 , pp. 12266-12275
    • Wyttenbach, T.1    Bowers, M.T.2
  • 39
    • 0025674590 scopus 로고
    • Probing conformational changes in proteins by mass spectrometry
    • S.K. Chowdhury, V. Katta, and B.T. Chait Probing conformational changes in proteins by mass spectrometry J. Am. Chem. Soc. 112 1990 9012 9013
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9012-9013
    • Chowdhury, S.K.1    Katta, V.2    Chait, B.T.3
  • 40
    • 80052093839 scopus 로고    scopus 로고
    • Detection of a protein conformational equilibrium by electrospray ionisation-ion mobility-mass spectrometry
    • M. Jenner, J. Ellis, W.-C. Huang, E.L. Raven, G.C.K. Roberts, and N.J. Oldham Detection of a protein conformational equilibrium by electrospray ionisation-ion mobility-mass spectrometry Angew. Chem. Int. Ed. 50 2011 8291 8294
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 8291-8294
    • Jenner, M.1    Ellis, J.2    Huang, W.-C.3    Raven, E.L.4    Roberts, G.C.K.5    Oldham, N.J.6
  • 42
  • 43
    • 0024742246 scopus 로고
    • Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition
    • E.I. Shakhnovich, and A.V. Finkelstein Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition Biopolymers 28 1989 1667 1680
    • (1989) Biopolymers , vol.28 , pp. 1667-1680
    • Shakhnovich, E.I.1    Finkelstein, A.V.2
  • 44
    • 0024745242 scopus 로고
    • Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution
    • A.V. Finkelstein, and E.I. Shakhnovich Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution Biopolymers 28 1989 1681 1694
    • (1989) Biopolymers , vol.28 , pp. 1681-1694
    • Finkelstein, A.V.1    Shakhnovich, E.I.2
  • 45
    • 84876593406 scopus 로고    scopus 로고
    • The how's and why's of protein folding intermediates
    • M. Tsytlonok, and L.S. Itzhaki The how's and why's of protein folding intermediates Arch. Biochem. Biophys. 531 2013 14 23
    • (2013) Arch. Biochem. Biophys. , vol.531 , pp. 14-23
    • Tsytlonok, M.1    Itzhaki, L.S.2
  • 48
    • 0034584873 scopus 로고    scopus 로고
    • The use of circular dichroism in the investigation of protein structure and function
    • S.M. Kelly, and N.C. Price The use of circular dichroism in the investigation of protein structure and function Curr. Protein Pept. Sci. 4 2000 349 384
    • (2000) Curr. Protein Pept. Sci. , vol.4 , pp. 349-384
    • Kelly, S.M.1    Price, N.C.2
  • 49
    • 77953905304 scopus 로고    scopus 로고
    • a values with continuous constant pH molecular dynamics
    • a values with continuous constant pH molecular dynamics Methods Enzymol. 466 2009 455 475
    • (2009) Methods Enzymol. , vol.466 , pp. 455-475
    • Wallace, J.A.1    Shen, J.K.2
  • 50
    • 79953701671 scopus 로고    scopus 로고
    • A survey of aspartate-phenylalanine and glutamate-phenylalanine interactions in the protein data bank: Searching for anion-π pairs
    • V. Philip, J. Harris, R. Adams, D. Nguyen, J. Spiers, J. Baudry, E.E. Howell, and R.J. Hinde A survey of aspartate-phenylalanine and glutamate-phenylalanine interactions in the protein data bank: searching for anion-π pairs Biochemistry 50 2011 2939 2950
    • (2011) Biochemistry , vol.50 , pp. 2939-2950
    • Philip, V.1    Harris, J.2    Adams, R.3    Nguyen, D.4    Spiers, J.5    Baudry, J.6    Howell, E.E.7    Hinde, R.J.8
  • 51
    • 0033040807 scopus 로고    scopus 로고
    • Characterization of a molten globule state of bovine carbonic anhydrase. III: Loss of asymmetrical environment of the aromatic residues has a profound effect on both the near- and far-UV CD spectrum
    • DOI 10.1016/S0167-4838(98)00283-0, PII S0167483898002830
    • K. Borén, P. Andersson, M. Larsson, and U. Carlsson Characterization of a molten globule state of bovine carbonic anhydrase III: loss of asymmetrical environment of the aromatic residues has a profound effect on both the near- and far-UV CD spectrum Biochim. Biophys. Acta 1430 1999 111 118 (Pubitemid 29132840)
    • (1999) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1430 , Issue.1 , pp. 111-118
    • Boren, K.1    Andersson, P.2    Larsson, M.3    Carlsson, U.4
  • 52
    • 0027298784 scopus 로고
    • Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities
    • A. Chakrabartty, T. Kortemme, S. Padmanabhan, and R.L. Baldwin Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities Biochemistry 32 1993 5560 5565 (Pubitemid 23178520)
    • (1993) Biochemistry , vol.32 , Issue.21 , pp. 5560-5565
    • Chakrabartty, A.1    Kortemme, T.2    Padmanabhan, S.3    Baldwin, R.L.4
  • 53
    • 77953832319 scopus 로고    scopus 로고
    • Near-infrared and mid-infrared Fourier transform vibrational circular dichroism of proteins in aqueous solution
    • S. Ma, T.B. Freedman, R.K. Dukor, and L.A. Nafie Near-infrared and mid-infrared Fourier transform vibrational circular dichroism of proteins in aqueous solution Appl. Spectrosc. 64 2010 615 626
    • (2010) Appl. Spectrosc. , vol.64 , pp. 615-626
    • Ma, S.1    Freedman, T.B.2    Dukor, R.K.3    Nafie, L.A.4
  • 54
    • 0025883964 scopus 로고
    • Effect of metal ion binding on the secondary structure of bovine α-lactalbumin as examined by infrared spectroscopy
    • S.J. Prestrelski, D.M. Byler, and M.P. Thompson Effect of metal ion binding on the secondary structure of bovine α-lactalbumin as examined by infrared spectroscopy Biochemistry 30 1991 8797 8804
    • (1991) Biochemistry , vol.30 , pp. 8797-8804
    • Prestrelski, S.J.1    Byler, D.M.2    Thompson, M.P.3
  • 55
    • 77957118527 scopus 로고    scopus 로고
    • Interplay between secondary and tertiary structure formation in protein folding cooperativity
    • T. Bereau, M. Bachmann, and M. Deserno Interplay between secondary and tertiary structure formation in protein folding cooperativity J. Am. Chem. Soc. 132 2010 13129 13131
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13129-13131
    • Bereau, T.1    Bachmann, M.2    Deserno, M.3
  • 56
    • 0001437708 scopus 로고    scopus 로고
    • FTIR-ATR and radiolabeling study of structural modifications during protein adsorption on hydrophilic surfaces. 2. The case of apo-α- lactalbumine
    • A. Bentaleb, A. Abele, Y. Haikel, P. Schaaf, and J.C. Voege FTIR-ATR and radiolabeling study of structural modifications during protein adsorption on hydrophilic surfaces. 2. The case of apo-α-lactalbumine Langmuir 15 1999 4930 4933
    • (1999) Langmuir , vol.15 , pp. 4930-4933
    • Bentaleb, A.1    Abele, A.2    Haikel, Y.3    Schaaf, P.4    Voege, J.C.5
  • 57
    • 0032005382 scopus 로고    scopus 로고
    • A new attenuated total reflectance fourier transform infrared spectroscopy method for the study of proteins in solution
    • DOI 10.1006/abio.1997.2486
    • K.A. Oberg, and A.L. Fink A new attenuated total reflectance Fourier transform infrared spectroscopy method for the study of proteins in solution Anal. Biochem. 256 1998 92 106 (Pubitemid 28080180)
    • (1998) Analytical Biochemistry , vol.256 , Issue.1 , pp. 92-106
    • Oberg, K.A.1    Fink, A.L.2
  • 58
    • 0035887070 scopus 로고    scopus 로고
    • Fourier transform infrared spectrometric analysis of protein conformation: Effect of sampling method and stress factors
    • DOI 10.1006/abio.2001.5337
    • M. van de Weert, P.I. Haris, W.E. Hennink, and D.J.A. Crommelin Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors Anal. Biochem. 297 2001 160 169 (Pubitemid 32989346)
    • (2001) Analytical Biochemistry , vol.297 , Issue.2 , pp. 160-169
    • Van De Weert, M.1    Haris, P.I.2    Hennink, W.E.3    Crommelin, D.J.A.4
  • 59
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • DOI 10.1016/S0304-4157(99)00004-0, PII S0304415799000040
    • E. Goormaghtigh, V. Raussens, and J.-M. Ruysschaert Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes Biochim. Biophys. Acta 1422 1999 105 185 (Pubitemid 29313327)
    • (1999) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1422 , Issue.2 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.-M.3
  • 60
    • 0032183033 scopus 로고    scopus 로고
    • Characteristic protein adhesion forces on glass and polystyrene substrates by atomic force microscopy
    • G. Sagvolden, I. Giaever, and J. Feder Characteristic protein adhesion forces on glass and polystyrene substrates by atomic force microscopy Langmuir 14 1998 5984 5987 (Pubitemid 128612918)
    • (1998) Langmuir , vol.14 , Issue.21 , pp. 5984-5987
    • Sagvolden, G.1    Giaever, I.2    Feder, J.3
  • 62
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • DOI 10.1017/S0033583502003815
    • A. Barth, and C. Zscherp What vibrations tell us about proteins Q. Rev. Biophys. 35 2002 369 430 (Pubitemid 36207229)
    • (2002) Quarterly Reviews of Biophysics , vol.35 , Issue.4 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 63
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • A.L. Fink Protein aggregation: folding aggregates, inclusion bodies and amyloid Fold. Des. 3 1998 R9 R23
    • (1998) Fold. Des. , vol.3
    • Fink, A.L.1
  • 65
    • 0035895427 scopus 로고    scopus 로고
    • Exploration of partially unfolded states of human α-lactalbumin by molecular dynamics simulation
    • DOI 10.1006/jmbi.2000.4337
    • E. Paci, L.J. Smith, C.M. Dobson, and M. Karplus Exploration of partially unfolded states of human α-lactalbumin by molecular dynamics simulation J. Mol. Biol. 306 2001 329 347 (Pubitemid 33032883)
    • (2001) Journal of Molecular Biology , vol.306 , Issue.2 , pp. 329-347
    • Paci, E.1    Smith, L.J.2    Dobson, C.M.3    Karplus, M.4
  • 66
    • 0033514289 scopus 로고    scopus 로고
    • Thermal and pH-induced conformational changes of a β-sheet protein monitored by infrared spectroscopy
    • R. Chehín, I. Iloro, M.J. Marcos, E. Villar, V.L. Shnyrov, and J.L. Arrondo Thermal and pH-induced conformational changes of a β-sheet protein monitored by infrared spectroscopy Biochemistry 38 1999 1525 1530
    • (1999) Biochemistry , vol.38 , pp. 1525-1530
    • Chehín, R.1    Iloro, I.2    Marcos, M.J.3    Villar, E.4    Shnyrov, V.L.5    Arrondo, J.L.6
  • 67
    • 79953190479 scopus 로고    scopus 로고
    • Adsorption behavior of human serum albumin on ATR crystal studied by in situ ATR/FTIR spectroscopy and two-dimensional correlation analysis
    • H. Huang, J. Xie, and H. Chen Adsorption behavior of human serum albumin on ATR crystal studied by in situ ATR/FTIR spectroscopy and two-dimensional correlation analysis Analyst 136 2011 1747 1752
    • (2011) Analyst , vol.136 , pp. 1747-1752
    • Huang, H.1    Xie, J.2    Chen, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.