메뉴 건너뛰기




Volumn 340, Issue 1, 2005, Pages 89-98

Probing conformational changes of proteins by quantitative second-derivative infrared spectroscopy

Author keywords

Infrared spectroscopy; Protein aggregation; Protein conformational change; Quantitative analysis; Second derivative analysis

Indexed keywords

AMINO ACIDS; CHEMICAL ANALYSIS; INFRARED SPECTROSCOPY; MAMMALS; SPECTRUM ANALYSIS;

EID: 15744400209     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2005.01.053     Document Type: Article
Times cited : (72)

References (33)
  • 1
    • 0001002352 scopus 로고
    • Conformational changes of proteins
    • R. Lumry, and H. Eyring Conformational changes of proteins J. Phys. Chem. 58 1954 110 120
    • (1954) J. Phys. Chem. , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 2
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • J.M. Kelly Alternative conformations of amyloidogenic proteins govern their behavior Curr. Opin. Struct. Biol. 6 1996 11 17
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 11-17
    • Kelly, J.M.1
  • 3
    • 1342302339 scopus 로고    scopus 로고
    • Conformational changes associated with protein-protein interactions
    • C.-S. Goh, D. Milburn, and M. Gerstein Conformational changes associated with protein-protein interactions Curr. Opin. Struct. Biol. 14 2004 104 109
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 104-109
    • Goh, C.-S.1    Milburn, D.2    Gerstein, M.3
  • 4
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • J.T. Pelton, and L.R. McLean Spectroscopic methods for analysis of protein secondary structure Anal. Biochem. 277 2002 167 176
    • (2002) Anal. Biochem. , vol.277 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 5
    • 0038096324 scopus 로고
    • Two-dimensional infrared spectroscopy
    • I. Noda Two-dimensional infrared spectroscopy J. Am. Chem. Soc. 111 1989 8116 8118
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8116-8118
    • Noda, I.1
  • 6
    • 0025434356 scopus 로고
    • Two-dimensional infrared (2D-IR) spectroscopy: Theory and applications
    • I. Noda Two-dimensional infrared (2D-IR) spectroscopy: theory and applications Appl. Spectrosc. 44 1990 550 561
    • (1990) Appl. Spectrosc. , vol.44 , pp. 550-561
    • Noda, I.1
  • 7
    • 33745563365 scopus 로고
    • Generalized two-dimensional correlation method applications to infrared, Raman, and other types of spectroscopy
    • I. Noda Generalized two-dimensional correlation method applications to infrared, Raman, and other types of spectroscopy Appl. Spectrosc. 47 1993 1329 1336
    • (1993) Appl. Spectrosc. , vol.47 , pp. 1329-1336
    • Noda, I.1
  • 8
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • H. Susi, and M. Byler Resolution-enhanced Fourier transform infrared spectroscopy of enzymes Methods Enzymol. 130 1986 290 311
    • (1986) Methods Enzymol. , vol.130 , pp. 290-311
    • Susi, H.1    Byler, M.2
  • 9
    • 0000316288 scopus 로고
    • Fourier transform infrared spectroscopic studies of lipids, polypeptides and proteins
    • M. Jackson, P.I. Haris, and D. Chapman Fourier transform infrared spectroscopic studies of lipids, polypeptides and proteins J. Mol. Struct. 214 1989 329 355
    • (1989) J. Mol. Struct. , vol.214 , pp. 329-355
    • Jackson, M.1    Haris, P.I.2    Chapman, D.3
  • 10
    • 0026731378 scopus 로고
    • Does Fourier-transform infrared spectroscopy provide useful information on protein structures?
    • P.I. Haris, and D. Chapman Does Fourier-transform infrared spectroscopy provide useful information on protein structures? Trends Biol. Sci. 17 1992 328 333
    • (1992) Trends Biol. Sci. , vol.17 , pp. 328-333
    • Haris, P.I.1    Chapman, D.2
  • 11
    • 0019599157 scopus 로고
    • Fourier transforms in the computation of self-deconvoluted and first-order derivative spectra of overlapped band contours
    • J.K. Kauppinen, D.J. Moffatt, H.H. Mantsch, and D.G. Cameron Fourier transforms in the computation of self-deconvoluted and first-order derivative spectra of overlapped band contours Anal. Chem. 53 1981 1454 1467
    • (1981) Anal. Chem. , vol.53 , pp. 1454-1467
    • Kauppinen, J.K.1    Moffatt, D.J.2    Mantsch, H.H.3    Cameron, D.G.4
  • 12
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • W.K. Surewicz, and H.H. Mantsch New insight into protein secondary structure from resolution-enhanced infrared spectra Biochim. Biophys. Acta 952 1988 115 130
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 13
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • J.L.R. Arrondo, A. Muga, J. Castresana, and F.M. Goni Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy Prog. Biophys. Mol. Biol. 59 1993 23 56
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.R.1    Muga, A.2    Castresana, J.3    Goni, F.M.4
  • 14
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • W.K. Surewicz, H.H. Mantsch, and D. Chapman Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment Biochemistry 32 1993 389 394
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 15
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • M. Jackson, and H.H. Mantsch The use and misuse of FTIR spectroscopy in the determination of protein structure Crit. Rev. Biochem. Mol. Biol. 30 1995 95 120
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 16
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • A. Dong, P. Huang, and W.S. Caughey Protein secondary structures in water from second-derivative amide I infrared spectra Biochemistry 29 1990 3303 3308
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 17
    • 0042823410 scopus 로고    scopus 로고
    • Two-dimensional infrared correlation spectroscopy study of the heat induced unfolding and aggregation process of Myoglobin
    • Y.-B. Yan, Q. Wang, H.-W. He, X.-Y. Hu, R.-Q. Zhang, and H.-M. Zhou Two-dimensional infrared correlation spectroscopy study of the heat induced unfolding and aggregation process of Myoglobin Biophys. J. 85 2003 1959 1967
    • (2003) Biophys. J. , vol.85 , pp. 1959-1967
    • Yan, Y.-B.1    Wang, Q.2    He, H.-W.3    Hu, X.-Y.4    Zhang, R.-Q.5    Zhou, H.-M.6
  • 18
    • 0000337013 scopus 로고
    • Fourier self-deconvolution: A method for resolving intrinsically overlapped bands
    • J.K. Kauppinen, D.J. Moffatt, H.H. Mantsch, and D.G. Cameron Fourier self-deconvolution: a method for resolving intrinsically overlapped bands Appl. Spectrosc. 35 1981 271 276
    • (1981) Appl. Spectrosc. , vol.35 , pp. 271-276
    • Kauppinen, J.K.1    Moffatt, D.J.2    Mantsch, H.H.3    Cameron, D.G.4
  • 20
    • 0033966584 scopus 로고    scopus 로고
    • Relationship between conformational stability and lyophilization-induced structural changes in chymotrypsin
    • K.G. Carrasquillo, C. Sanchez, and K. Griebenow Relationship between conformational stability and lyophilization-induced structural changes in chymotrypsin Biotechnol. Appl. Biochem. 31 2000 41 53
    • (2000) Biotechnol. Appl. Biochem. , vol.31 , pp. 41-53
    • Carrasquillo, K.G.1    Sanchez, C.2    Griebenow, K.3
  • 22
    • 0016373048 scopus 로고
    • Circular dichroism and proton magnetic resonance studies of random chain poly-l-lysine
    • R.M. Epand, G.E. Wheeler, and M.A. Moscarello Circular dichroism and proton magnetic resonance studies of random chain poly-l-lysine Biopolymers 13 1974 359 369
    • (1974) Biopolymers , vol.13 , pp. 359-369
    • Epand, R.M.1    Wheeler, G.E.2    Moscarello, M.A.3
  • 23
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • A. Barth The infrared absorption of amino acid side chains Prog. Biophys. Mol. Biol. 74 2000 141 173
    • (2000) Prog. Biophys. Mol. Biol. , vol.74 , pp. 141-173
    • Barth, A.1
  • 24
    • 1542724787 scopus 로고    scopus 로고
    • Chain-length dependence of α-Helix to β-Sheet transition in polylysine: Model of protein aggregation studied by temperature-tuned FTIR spectroscopy
    • W. Dzwolak, T. Muraki, and M. Kato Chain-length dependence of α-Helix to β-Sheet transition in polylysine: model of protein aggregation studied by temperature-tuned FTIR spectroscopy Biopolymers 73 2004 463 469
    • (2004) Biopolymers , vol.73 , pp. 463-469
    • Dzwolak, W.1    Muraki, T.2    Kato, M.3
  • 25
    • 0034623286 scopus 로고    scopus 로고
    • Entrapping intermediates of thermal aggregation in α-helical proteins with low concentration of guanidine hydrochloride
    • A. Dong, T.W. Randolph, and J.F. Carpenter Entrapping intermediates of thermal aggregation in α-helical proteins with low concentration of guanidine hydrochloride J. Biol. Chem. 275 2000 27689 27693
    • (2000) J. Biol. Chem. , vol.275 , pp. 27689-27693
    • Dong, A.1    Randolph, T.W.2    Carpenter, J.F.3
  • 26
    • 1542345526 scopus 로고    scopus 로고
    • Protein thermal aggregation involves distinct regions: Sequential events in the heat-induced unfolding and aggregation of hemoglobin
    • Y.-B. Yan, Q. Wang, H.-W. He, and H.-M. Zhou Protein thermal aggregation involves distinct regions: sequential events in the heat-induced unfolding and aggregation of hemoglobin Biophys. J. 86 2004 1682 1690
    • (2004) Biophys. J. , vol.86 , pp. 1682-1690
    • Yan, Y.-B.1    Wang, Q.2    He, H.-W.3    Zhou, H.-M.4
  • 29
    • 0019536747 scopus 로고
    • Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels
    • A.H. Clark, D.H.P. Saunderson, and A. Suggett Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels Int. J. Peptide Protein Res. 17 1981 353 364
    • (1981) Int. J. Peptide Protein Res. , vol.17 , pp. 353-364
    • Clark, A.H.1    Saunderson, D.H.P.2    Suggett, A.3
  • 30
    • 0000027238 scopus 로고    scopus 로고
    • Interactions involved in the gelation of bovine serum albumin
    • J.I. Boye, I. Alli, and A.A. Ismail Interactions involved in the gelation of bovine serum albumin J. Agric. Food. Chem. 44 1996 996 1004
    • (1996) J. Agric. Food. Chem. , vol.44 , pp. 996-1004
    • Boye, J.I.1    Alli, I.2    Ismail, A.A.3
  • 31
    • 0036739301 scopus 로고    scopus 로고
    • Two-dimensional attenuated total reflection/infrared correlation spectroscopy studies on concentration and heat-induced structural changes of human serum albumin in aqueous solutions
    • Y.Q. Wu, K. Murayama, B. Czarnik-Matusewicz, and Y. Ozaki Two-dimensional attenuated total reflection/infrared correlation spectroscopy studies on concentration and heat-induced structural changes of human serum albumin in aqueous solutions Appl. Spectrosc. 56 2002 1186 1193
    • (2002) Appl. Spectrosc. , vol.56 , pp. 1186-1193
    • Wu, Y.Q.1    Murayama, K.2    Czarnik-Matusewicz, B.3    Ozaki, Y.4
  • 32
    • 1242271236 scopus 로고    scopus 로고
    • Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering
    • V. Militello, C. Casarino, A. Emanuele, A. Giostra, F. Pullara, and M. Leone Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering Biophys. Chem. 107 2004 175 187
    • (2004) Biophys. Chem. , vol.107 , pp. 175-187
    • Militello, V.1    Casarino, C.2    Emanuele, A.3    Giostra, A.4    Pullara, F.5    Leone, M.6
  • 33
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shifts and protein secondary structure
    • D.S. Wishart,, B.D. Sykes, and F.M. Richards Relationship between nuclear magnetic resonance chemical shifts and protein secondary structure J. Mol. Biol. 222 1991 311 333
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.