메뉴 건너뛰기




Volumn 44, Issue 49, 2005, Pages 15997-16006

Temperature-induced molten globule-like state in human α1- acid glycoprotein: An infrared spectroscopic study

Author keywords

[No Author keywords available]

Indexed keywords

FOURIER TRANSFORM INFRARED SPECTROSCOPY; SPECTROSCOPIC ANALYSIS; THERMAL EFFECTS;

EID: 28944454419     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051512z     Document Type: Article
Times cited : (30)

References (63)
  • 1
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: Structure and function
    • Flower, D. R. (1996) The lipocalin protein family: structure and function, Biochem. J. 318 (Part 1), 1-14.
    • (1996) Biochem. J. , vol.318 , Issue.PART 1 , pp. 1-14
    • Flower, D.R.1
  • 2
    • 0017263227 scopus 로고
    • Steroid-protein interactions. XXXIV. Chemical modification of alpha 1-acid glycoprotein for characterization of the progesterone binding site
    • Kute, T., and Westphal, U. (1976) Steroid-protein interactions. XXXIV. Chemical modification of alpha 1-acid glycoprotein for characterization of the progesterone binding site, Biochim. Biophys. Acta 420, 195-213.
    • (1976) Biochim. Biophys. Acta , vol.420 , pp. 195-213
    • Kute, T.1    Westphal, U.2
  • 5
    • 0020319277 scopus 로고
    • The binding of spin-labeled propranolol and spin-labeled progesterone by orosomucoid
    • Kirley, T. L., Sprague, E. D., and Halsall, H. B. (1982) The binding of spin-labeled propranolol and spin-labeled progesterone by orosomucoid. Biophys. Chem. 15, 209-216.
    • (1982) Biophys. Chem. , vol.15 , pp. 209-216
    • Kirley, T.L.1    Sprague, E.D.2    Halsall, H.B.3
  • 6
    • 0023690101 scopus 로고
    • Drug binding to human alpha-1-acid glycoprotein in health and disease
    • Kremer, J. M., Wilting, J., and Janssen, L. H. (1988) Drug binding to human alpha-1-acid glycoprotein in health and disease. Pharmacol. Rev. 40, 1-47.
    • (1988) Pharmacol. Rev. , vol.40 , pp. 1-47
    • Kremer, J.M.1    Wilting, J.2    Janssen, L.H.3
  • 7
    • 0034894719 scopus 로고    scopus 로고
    • Human alpha-1-glycoprotein and its interactions with drugs
    • Israili, Z. H., and Dayton, P. G. (2001) Human alpha-1-glycoprotein and its interactions with drugs, Drug Metab. Rev. 33, 161-235.
    • (2001) Drug Metab. Rev. , vol.33 , pp. 161-235
    • Israili, Z.H.1    Dayton, P.G.2
  • 8
  • 9
    • 0037301226 scopus 로고    scopus 로고
    • Alpha(1)-acid glycoprotein: An acute phase protein with inflammatory and immunomodulating properties
    • Hochepied, T., Berger, F. G., Baumann, H., and Libert, C. (2003) Alpha(1)-acid glycoprotein: an acute phase protein with inflammatory and immunomodulating properties, Cytokine Growth Factor Rev. 14, 25-34.
    • (2003) Cytokine Growth Factor Rev. , vol.14 , pp. 25-34
    • Hochepied, T.1    Berger, F.G.2    Baumann, H.3    Libert, C.4
  • 10
    • 0022527659 scopus 로고
    • Thermal stability and ligand-binding properties of human plasma alpha 1-acid glycoprotein (orosomucoid) as determined with fluorescent probes
    • Busby, T. F., and Ingham, K. C. (1986) Thermal stability and ligand-binding properties of human plasma alpha 1-acid glycoprotein (orosomucoid) as determined with fluorescent probes, Biochim. Biophys. Acta 871, 61-71.
    • (1986) Biochim. Biophys. Acta , vol.871 , pp. 61-71
    • Busby, T.F.1    Ingham, K.C.2
  • 12
    • 12244257488 scopus 로고    scopus 로고
    • Thermal stability of the human blood serum acid alpha-(1)-glycoprotein in acidic media
    • Hofbauerova, K., Kopecky, V., Jr., Sykora, J., and Karpenko, V. (2003) Thermal stability of the human blood serum acid alpha-(1)-glycoprotein in acidic media, Biophys. Chem. 103, 25-33.
    • (2003) Biophys. Chem. , vol.103 , pp. 25-33
    • Hofbauerova, K.1    Kopecky Jr., V.2    Sykora, J.3    Karpenko, V.4
  • 13
    • 0025025938 scopus 로고
    • Unfolding behavior of human alpha 1-acid glycoprotein is compatible with a loosely folded region in its polypeptide chain
    • Rojo-Dominguez, A., Zubillaga-Luna, R., and Hernandez-Arana, A. (1990) Unfolding behavior of human alpha 1-acid glycoprotein is compatible with a loosely folded region in its polypeptide chain, Biochemistry 29, 8689-8695.
    • (1990) Biochemistry , vol.29 , pp. 8689-8695
    • Rojo-Dominguez, A.1    Zubillaga-Luna, R.2    Hernandez-Arana, A.3
  • 14
    • 0028852391 scopus 로고
    • Heat denaturation of human orosomucoid in water/methanol mixtures
    • Kodicek, M., Infanzon, A., and Karpenko, V. (1995) Heat denaturation of human orosomucoid in water/methanol mixtures, Biochim. Biophys. Acta 1246, 10-16.
    • (1995) Biochim. Biophys. Acta , vol.1246 , pp. 10-16
    • Kodicek, M.1    Infanzon, A.2    Karpenko, V.3
  • 15
    • 0017857378 scopus 로고
    • Circular dichroism studies on the effects of ethanol on the conformation of alpha 1-acid glycoprotein, alpha 1-antitrypsin, deoxyribonuclease, pepsinogen, soybean trypsin inhibitor and unfolded ribonucleases
    • Jirgensons, B. (1978) Circular dichroism studies on the effects of ethanol on the conformation of alpha 1-acid glycoprotein, alpha 1-antitrypsin, deoxyribonuclease, pepsinogen, soybean trypsin inhibitor and unfolded ribonucleases, Biochim. Biophys. Acta 534, 123-131.
    • (1978) Biochim. Biophys. Acta , vol.534 , pp. 123-131
    • Jirgensons, B.1
  • 17
    • 0032932846 scopus 로고    scopus 로고
    • Porcine odorant-binding protein: Structural stability and ligand affinities measured by Fourier-transform infrared spectroscopy and fluorescence spectroscopy
    • Paolini, S., Tanfani, F., Fini, C., Bertoli, E., and Paolo, P. (1999) Porcine odorant-binding protein: structural stability and ligand affinities measured by Fourier-transform infrared spectroscopy and fluorescence spectroscopy, Biochim. Biophys. Acta 1431, 179-188.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 179-188
    • Paolini, S.1    Tanfani, F.2    Fini, C.3    Bertoli, E.4    Paolo, P.5
  • 18
    • 0342862068 scopus 로고
    • Solvent deuterium isotope effects on acid-base equilibria
    • Salomaa, P., Schaleger, L. L., and Long, F. A. (1964) Solvent deuterium isotope effects on acid-base equilibria, J. Am. Chem. Soc. 86, 1-7.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 1-7
    • Salomaa, P.1    Schaleger, L.L.2    Long, F.A.3
  • 19
    • 0030961931 scopus 로고    scopus 로고
    • Reduced beta-strand content in apoprotein B-100 in smaller and denser low-density lipoprotein subclasses as probed by Fourier-transform infrared spectroscopy
    • Tanfani, F., Galeazzi, T., Curatola, G., Bertoli, E., and Ferretti, G. (1997) Reduced beta-strand content in apoprotein B-100 in smaller and denser low-density lipoprotein subclasses as probed by Fourier-transform infrared spectroscopy, Biochem. J. 322 (Part 3), 765-769.
    • (1997) Biochem. J. , vol.322 , Issue.PART 3 , pp. 765-769
    • Tanfani, F.1    Galeazzi, T.2    Curatola, G.3    Bertoli, E.4    Ferretti, G.5
  • 20
    • 0001119282 scopus 로고
    • Infrared measurement of peptide hydrogen exchange in rhodopsin
    • Osborne, H. B., and Nabedryk-Viala, E. (1982) Infrared measurement of peptide hydrogen exchange in rhodopsin, Methods Enzymol. 88, 676-680.
    • (1982) Methods Enzymol. , vol.88 , pp. 676-680
    • Osborne, H.B.1    Nabedryk-Viala, E.2
  • 21
    • 0036231272 scopus 로고    scopus 로고
    • Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin
    • Meersman, F., Smeller, L., and Heremans, K. (2002) Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin, Biophys. J. 82, 2635-2644.
    • (2002) Biophys. J. , vol.82 , pp. 2635-2644
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 22
    • 0028948157 scopus 로고
    • Surface-core relationships in human low-density lipoprotein as studied by infrared spectroscopy
    • Banuelos, S., Arrondo, J. L., Goni, F. M., and Pifat, G. (1995) Surface-core relationships in human low-density lipoprotein as studied by infrared spectroscopy, J. Biol. Chem. 270, 9192-9196.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9192-9196
    • Banuelos, S.1    Arrondo, J.L.2    Goni, F.M.3    Pifat, G.4
  • 23
    • 0034237803 scopus 로고    scopus 로고
    • Steady-state and time-resolved fluorescence of albumins interacting with N-oleylethanolamine, a component of the endogenous N-acylethanolamines
    • Zolese, G., Falcioni, G., Bertoli, E., Galeazzi, R., Wozniak, M., Wypych, Z., Gratton, E., and Ambrosini, A. (2000) Steady-state and time-resolved fluorescence of albumins interacting with N-oleylethanolamine, a component of the endogenous N-acylethanolamines, Proteins 40, 39-48.
    • (2000) Proteins , vol.40 , pp. 39-48
    • Zolese, G.1    Falcioni, G.2    Bertoli, E.3    Galeazzi, R.4    Wozniak, M.5    Wypych, Z.6    Gratton, E.7    Ambrosini, A.8
  • 24
    • 33745563365 scopus 로고
    • Generalized two-dimensional correlation method applicable to infrared, Raman, and other types of spectroscopy
    • Noda, I. (1993) Generalized two-dimensional correlation method applicable to infrared, Raman, and other types of spectroscopy, Appl. Spectrosc. 47, 1329-1336.
    • (1993) Appl. Spectrosc. , vol.47 , pp. 1329-1336
    • Noda, I.1
  • 26
    • 0035699831 scopus 로고    scopus 로고
    • Global phase angle description
    • Morita, S., Ozaki, Y., and Noda, I. (2001) Global phase angle description, Appl. Spectrosc. 55, 1618-1621.
    • (2001) Appl. Spectrosc. , vol.55 , pp. 1618-1621
    • Morita, S.1    Ozaki, Y.2    Noda, I.3
  • 27
    • 0034274524 scopus 로고    scopus 로고
    • Moving-window two-dimensional correlation spectroscopy, Vib
    • Thomas, M., and Richardson, H. H. (2000) Moving-window two-dimensional correlation spectroscopy, Vib. Spectrosc. 24, 137-146.
    • (2000) Spectrosc. , vol.24 , pp. 137-146
    • Thomas, M.1    Richardson, H.H.2
  • 28
    • 0033539558 scopus 로고    scopus 로고
    • Two-dimensional IR correlation spectroscopy: Sequential events in the unfolding process of the lambda cro-V55C represser protein
    • Fabian, H., Mantsch, H. H., and Schultz, C. P. (1999) Two-dimensional IR correlation spectroscopy: sequential events in the unfolding process of the lambda cro-V55C represser protein, Proc. Natl. Acad. Sci. U.S.A. 96, 13153-13158.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13153-13158
    • Fabian, H.1    Mantsch, H.H.2    Schultz, C.P.3
  • 30
    • 2442452683 scopus 로고    scopus 로고
    • Use of the phase diagram method to analyze the protein unfolding-refolding reactions: Fishing out the "invisible" intermediates
    • Kuznetsova, I. M., Turoverov, K. K., and Uversky, V. N. (2004) Use of the phase diagram method to analyze the protein unfolding-refolding reactions: fishing out the "invisible" intermediates, J. Proteome Res. 3, 485-494.
    • (2004) J. Proteome Res. , vol.3 , pp. 485-494
    • Kuznetsova, I.M.1    Turoverov, K.K.2    Uversky, V.N.3
  • 31
    • 0043069834 scopus 로고    scopus 로고
    • Structural and thermal stability analysis of Escherichia coli and Alicyclobacillus acidocaldarius thioredoxin revealed a molten globule-like state in thermal denaturation pathway of the proteins: An infrared spectroscopic study
    • Pedone, E., Bartolucci, S., Rossi, M., Pierfederici, F. M., Scire, A., Cacciamani, T., and Tanfani, F. (2003) Structural and thermal stability analysis of Escherichia coli and Alicyclobacillus acidocaldarius thioredoxin revealed a molten globule-like state in thermal denaturation pathway of the proteins: an infrared spectroscopic study, Biochem. J. 373, 875-883.
    • (2003) Biochem. J. , vol.373 , pp. 875-883
    • Pedone, E.1    Bartolucci, S.2    Rossi, M.3    Pierfederici, F.M.4    Scire, A.5    Cacciamani, T.6    Tanfani, F.7
  • 32
    • 10844275618 scopus 로고    scopus 로고
    • Binding of glutamine to glutamine-binding protein from Escherichia coli induces changes in protein structure and increases protein stability
    • D'Auria, S., Scire, A., Varriale, A., Scognamiglio, V., Staiano, M., Ausili, A., Marabotti, A., Rossi, M., and Tanfani, F. (2005) Binding of glutamine to glutamine-binding protein from Escherichia coli induces changes in protein structure and increases protein stability, Proteins 58, 80-87.
    • (2005) Proteins , vol.58 , pp. 80-87
    • D'Auria, S.1    Scire, A.2    Varriale, A.3    Scognamiglio, V.4    Staiano, M.5    Ausili, A.6    Marabotti, A.7    Rossi, M.8    Tanfani, F.9
  • 33
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler, D. M., and Susi, H. (1986) Examination of the secondary structure of proteins by deconvolved FTIR spectra, Biopolymers 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 34
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • Arrondo, J. L., Muga, A., Castresana, J., and Goni, F. M. (1993) Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy, Prog. Biophys. Mol. Biol. 59, 23-56.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.1    Muga, A.2    Castresana, J.3    Goni, F.M.4
  • 35
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • Surewicz, W. K., and Manisch, H. H. (1988) New insight into protein secondary structure from resolution-enhanced infrared spectra, Biochim. Biophys. Acta 952, 115-130.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Manisch, H.H.2
  • 36
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S., and Bandekar, J. (1986) Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins, Adv. Protein Chem. 38, 181-364.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 37
    • 0016797947 scopus 로고
    • Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water
    • Chirgadze, Y. N., Fedorov, O. V., and Trushina, N. P. (1975) Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water, Biopolymers 14, 679-694.
    • (1975) Biopolymers , vol.14 , pp. 679-694
    • Chirgadze, Y.N.1    Fedorov, O.V.2    Trushina, N.P.3
  • 38
    • 0017288712 scopus 로고
    • Infrared spectra and resonance interaction of amide-I vibration of the antiparallel-chain pleated sheet
    • Chirgadze, Y. N., and Nevskaya, N. A. (1976) Infrared spectra and resonance interaction of amide-I vibration of the antiparallel-chain pleated sheet, Biopolymers 15, 607-625.
    • (1976) Biopolymers , vol.15 , pp. 607-625
    • Chirgadze, Y.N.1    Nevskaya, N.A.2
  • 40
    • 0027216215 scopus 로고
    • Fourier transform infrared spectroscopy and electrochemistry of the primary electron donor in Rhodobacter sphaeroides and Rhodopseudomonas viridis reaction centers: Vibrational modes of the pigments in situ and evidence for protein and water modes affected by P+ formation
    • Leonhard, M., and Mantele, W. (1993) Fourier transform infrared spectroscopy and electrochemistry of the primary electron donor in Rhodobacter sphaeroides and Rhodopseudomonas viridis reaction centers: vibrational modes of the pigments in situ and evidence for protein and water modes affected by P+ formation, Biochemistry 32, 4532-4538.
    • (1993) Biochemistry , vol.32 , pp. 4532-4538
    • Leonhard, M.1    Mantele, W.2
  • 41
    • 0026491207 scopus 로고
    • Structural and functional relationships in DnaK and DnaK756 heat-shock proteins from Escherichia coli
    • Banecki, B., Zylicz, M., Bertoli, E., and Tanfani, F. (1992) Structural and functional relationships in DnaK and DnaK756 heat-shock proteins from Escherichia coli, J. Biol. Chem. 267, 25051-25058.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25051-25058
    • Banecki, B.1    Zylicz, M.2    Bertoli, E.3    Tanfani, F.4
  • 42
    • 0025434356 scopus 로고
    • Two-dimensional infrared (2D IR) spectroscopy: Theory and applications
    • Noda, I. (1990) Two-dimensional infrared (2D IR) spectroscopy: theory and applications, Appl. Spectrosc. 44, 550-561.
    • (1990) Appl. Spectrosc. , vol.44 , pp. 550-561
    • Noda, I.1
  • 43
    • 3242839920 scopus 로고    scopus 로고
    • Potential of generalised two-dimensional correlation spectroscopy in the near infrared region
    • Ozaki, Y., and Noda, I. (1996) Potential of generalised two-dimensional correlation spectroscopy in the near infrared region, J. Near Infrared Spectrosc. 4, 85-99.
    • (1996) J. Near Infrared Spectrosc. , vol.4 , pp. 85-99
    • Ozaki, Y.1    Noda, I.2
  • 44
    • 33644484271 scopus 로고
    • Two-dimensional Fourier transform near-infrared correlation spectroscopy studies of temperature-dependent spectral variations of oleyl alcohol
    • Noda, I., Liu, Y., Ozaki, Y., and Czarnecki, M. A. (1995) Two-dimensional Fourier transform near-infrared correlation spectroscopy studies of temperature-dependent spectral variations of oleyl alcohol, J. Phys. Chem. 99, 3068-3073.
    • (1995) J. Phys. Chem. , vol.99 , pp. 3068-3073
    • Noda, I.1    Liu, Y.2    Ozaki, Y.3    Czarnecki, M.A.4
  • 45
    • 0346004224 scopus 로고    scopus 로고
    • Two-dimensional correlation spectroscopy study of temperature-dependent spectral variations of N-methylacetamide in the pure liquid state. 2. Two-dimensional Raman and infrared-Raman heterospectral analysis
    • Noda, I., Liu, Y., and Ozaki, Y. (1996) Two-dimensional correlation spectroscopy study of temperature-dependent spectral variations of N-methylacetamide in the pure liquid state. 2. Two-dimensional Raman and infrared-Raman heterospectral analysis, J. Phys. Chem. 100, 8674-8680.
    • (1996) J. Phys. Chem. , vol.100 , pp. 8674-8680
    • Noda, I.1    Liu, Y.2    Ozaki, Y.3
  • 46
    • 0347265166 scopus 로고    scopus 로고
    • Two-dimensional correlation spectroscopy study of temperature-dependent spectral variations of N-methylacetamide in the pure liquid state. 1. Two-dimensional infrared analysis
    • Noda, I., Liu, Y., and Ozaki, Y. (1996) Two-dimensional correlation spectroscopy study of temperature-dependent spectral variations of N-methylacetamide in the pure liquid state. 1. Two-dimensional infrared analysis, J. Phys. Chem. 100, 8665-8673.
    • (1996) J. Phys. Chem. , vol.100 , pp. 8665-8673
    • Noda, I.1    Liu, Y.2    Ozaki, Y.3
  • 47
    • 0035902439 scopus 로고    scopus 로고
    • Two-dimensional infrared correlation spectroscopy as a probe of sequential events in the thermal unfolding of cytochromes c
    • Filosa, A., Wang, Y., Ismail, A. A., and English, A. M. (2001) Two-dimensional infrared correlation spectroscopy as a probe of sequential events in the thermal unfolding of cytochromes c, Biochemistry 40, 8256-8263.
    • (2001) Biochemistry , vol.40 , pp. 8256-8263
    • Filosa, A.1    Wang, Y.2    Ismail, A.A.3    English, A.M.4
  • 48
    • 0034957763 scopus 로고    scopus 로고
    • Two-dimensional infrared correlation spectroscopy study of the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol
    • Paquet, M. J., Laviolette, M., Pezolet, M., and Auger, M. (2001) Two-dimensional infrared correlation spectroscopy study of the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol, Biophys. J. 81, 305-312.
    • (2001) Biophys. J. , vol.81 , pp. 305-312
    • Paquet, M.J.1    Laviolette, M.2    Pezolet, M.3    Auger, M.4
  • 50
    • 0031019791 scopus 로고    scopus 로고
    • Molten globule of human alpha-lactalbumin: Hydration, density, and compressibility of the interior
    • Kharakoz, D. P., and Bychkova, V. E. (1997) Molten globule of human alpha-lactalbumin: hydration, density, and compressibility of the interior, Biochemistry 36, 1882-1890.
    • (1997) Biochemistry , vol.36 , pp. 1882-1890
    • Kharakoz, D.P.1    Bychkova, V.E.2
  • 51
    • 0034581317 scopus 로고    scopus 로고
    • The energy landscape theory of protein folding: Insights into folding mechanisms and scenarios
    • Onuchic, J. N., Nymeyer, H., Garcia, A. E., Chahine, J., and Socci, N. D. (2000) The energy landscape theory of protein folding: insights into folding mechanisms and scenarios, Adv. Protein Chem. 53, 87-152.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 87-152
    • Onuchic, J.N.1    Nymeyer, H.2    Garcia, A.E.3    Chahine, J.4    Socci, N.D.5
  • 52
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of alpha-lactalbumin
    • Kuwajima, K. (1996) The molten globule state of alpha-lactalbumin, FASEB J. 10, 102-109.
    • (1996) FASEB J. , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 53
    • 0642333026 scopus 로고    scopus 로고
    • Oxygen-17 nuclear magnetic resonance studies of bovine and caprine casein hydration and activity in deuterated sugar solutions
    • Mora-Gutierrez, A., Kumosinski, T. F., and Farrell, H. M. J. (1997) Oxygen-17 nuclear magnetic resonance studies of bovine and caprine casein hydration and activity in deuterated sugar solutions, J. Agric. Food Chem. 45, 4545-4553.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 4545-4553
    • Mora-Gutierrez, A.1    Kumosinski, T.F.2    Farrell, H.M.J.3
  • 54
    • 0033871781 scopus 로고    scopus 로고
    • Protein folding intermediates and pathways studied by hydrogen exchange
    • Englander, S. W. (2000) Protein folding intermediates and pathways studied by hydrogen exchange, Annu. Rev. Biophys. Biomol. Struct. 29, 213-238.
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 213-238
    • Englander, S.W.1
  • 57
    • 14844304355 scopus 로고    scopus 로고
    • Equilibrium titrations of acid-induced unfolding-refolding and salt-induced molten globule of cytochrome c by FT-IR spectroscopy
    • Dong, A., and Lam, T. (2005) Equilibrium titrations of acid-induced unfolding-refolding and salt-induced molten globule of cytochrome c by FT-IR spectroscopy, Arch. Biochem. Biophys. 436, 154-160.
    • (2005) Arch. Biochem. Biophys. , vol.436 , pp. 154-160
    • Dong, A.1    Lam, T.2
  • 58
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis
    • Qi, X. L., Holt, C., McNulty, D., Clarke, D. T., Brownlow, S., and Jones, G. R. (1997) Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis, Biochem. J. 324 (Part 1), 341-346.
    • (1997) Biochem. J. , vol.324 , Issue.PART 1 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    McNulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 59
    • 0029917563 scopus 로고    scopus 로고
    • Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface
    • Bychkova, V. E., Dujsekina, A. E., Klenin, S. I., Tiktopulo, E. I., Uversky, V. N., and Ptitsyn, O. B. (1996) Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface, Biochemistry 35, 6058-6063.
    • (1996) Biochemistry , vol.35 , pp. 6058-6063
    • Bychkova, V.E.1    Dujsekina, A.E.2    Klenin, S.I.3    Tiktopulo, E.I.4    Uversky, V.N.5    Ptitsyn, O.B.6
  • 61
    • 0023710642 scopus 로고
    • The "molten globule" state is involved in the translocation of proteins across membranes?
    • Bychkova, V. E., Pain, R. H., and Ptitsyn, O. B. (1988) The "molten globule" state is involved in the translocation of proteins across membranes?, FEBS Lett. 238, 231-234.
    • (1988) FEBS Lett. , vol.238 , pp. 231-234
    • Bychkova, V.E.1    Pain, R.H.2    Ptitsyn, O.B.3
  • 62
    • 0032491199 scopus 로고    scopus 로고
    • Ligand-induced conformational change in transferrins: Crystal structure of the open form of the N-terminal half-molecule of human transferrin
    • Jeffrey, P. D., Bewley, M. C., MacGillivray, R. T., Mason, A. B., Woodworth, R. C., and Baker, E. N. (1998) Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin, Biochemistry 37, 13978-13986.
    • (1998) Biochemistry , vol.37 , pp. 13978-13986
    • Jeffrey, P.D.1    Bewley, M.C.2    MacGillivray, R.T.3    Mason, A.B.4    Woodworth, R.C.5    Baker, E.N.6
  • 63
    • 4043117594 scopus 로고    scopus 로고
    • Binding of alpha1-acid glycoprotein to membrane results in a unique structural change and ligand release
    • Nishi, K., Maruyama, T., Halsall, H. B., Handa, T., and Otagiri, M. (2004) Binding of alpha1-acid glycoprotein to membrane results in a unique structural change and ligand release, Biochemistry 43, 10513-10519.
    • (2004) Biochemistry , vol.43 , pp. 10513-10519
    • Nishi, K.1    Maruyama, T.2    Halsall, H.B.3    Handa, T.4    Otagiri, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.