TWO-DIMENSIONALINFRARED CORRELATION SPECTROSCOPY STUDIES OF PROTEINS IN AQUEOUS SOLUTIONS

[in Chinese]; [in Chinese]

[1] Clark R J H; Hester R E; eds. Biomolecular Spectroscopy. Chichester: John Wiley & Sons; 1993; 20: Part A; 21: Part B

[2] Havel H A. Spectroscopic Methods for Determining Protein Structure in Solution. Chichester: John Wiley & Sons; 1995

[3] Jackson M; Mantsch H H. The use and misuse of FTIR spectroscopy in the determination of protein structure. Critical Rev. Biochem. Mol. Biol.; 1995; 30: 95

[4] Torii H; Tasumi M. In: Infrared Spectroscopy of Biomolecules. Mantsch H H; Chapman D; eds. New York: John Wiley & Sons; 1996: 1

[5] Haris P I; Chapman D. Infrared Spectroscopy of Biomolecules. New York: John Wiley & Sons; 1996: 239

[6] ］Noda I. Generalized two-dimensional correlation method applicable to infrared; Raman; and other types of spectroscopy. Appl. Spectrosc; 1993; 47: 550

[7] Noda; I. Determination of two-dimensional correlation spectra using the hilbert transform. Appl. Spectrosc; 2000; 54: 994

[8] Nabet A; Pezolet M. Two-dimensional FTIR spectroscopy: a powerful method to study the secondary structure of proteins using H-D exchange.Appl. Spectrosc; 1997; 51: 466

[9] Swellers L; Heremans K. 2D FT-IR spectroscopy analysis of the pressure-induced changes in proteins.Vib. Spectrosc.; 1999; 19: 375

[10] Dzwolak W; Kato M; Shimizu A; et al. Comparative two-dimensional fourier transform infrared correlation spectroscopic study on the spontaneous pressure-and temperature-enhanced H/D exchange in α-lactalbumin. Appl. Spectrosc.; 2000; 54: 963

[11] Paquet M J; Auger M; Pezolet M. 2D-IR study of the aggregation of lipid-bound cytochrome c. Ozaki Y; Noda I; eds. AIP Conference Proceedings. New York: American Institute of Physics; 2000; 503: 103

[12] Schultz C P; Fabian H; Mantsch H H. Two-dimensional mid-IR and near-IR correlation spectra of ribonuclease A: using overtones and combination modes to monitor changes in secondary structure. Biospectrosc.; 1998; 4: S19

[13] Czarnik-Matusewicz B; Murayama K; Wu Y; et al. Two-dimensional attenuated total reflection/infrared correlation spectroscopy of adsorption-induced and concentration-dependent spectral variations of β-lactoglobulin in aqueous solutions. J. Phys. Chem. B; 2000; 104: 7803

[15] Jung Y M; Czarnik-Matusewicz B; Ozaki Y. Two-dimensional infrared; two-dimensional Raman; and two-dimensional infrared and Raman heterospectral correlation studies of secondary structure of β-lactoglobulin in buffer solutions. J. Phys. Chem. B; 2000; 104: 7812

[16] Wu Y; Czarnik-Matusewicz B; Murayama K; et al. Two-dimensional near-infrared spectroscopy study of human serum albumin in aqueous solutions: using overtones and combination modes to monitor temperature-dependent changes in the secondary structure. J. Phys. Chem. B; 2000; 104: 5840

[17] Wu Y; Jiang J; Ozaki Y. A New Possibility of Generalized Two-Dimensional Correlation Spectroscopy: Hybrid Two-Dimensional Correlation Spectroscopy. J. Phys. Chem.A; 2002; 106: 2422.

[18] Ozaki Y; Noda I; eds. Two-dimensional correlation spectroscopy. AIP Conference Proceedings.New York:American Institute of Physics; 2000: 503

[19] Wu Y; Murayamak; Czarnik-Matusewicz B; et al. 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; 2002; 56:1186

[20] Crowfoot D M; Riley D P. Structure of β-lactoglobulin.Nature; 1938; 141: 521

[21] Peters T Jr. All About Albumin; Biochemistry; Genetics; and Medical Applications.New York:Academic Press; 1994: 35

[22] Protein Data Bank; Department of Chemistry; Brookhaven National Laboratory; Upton;NY 11973; USA; HTTP://WWW.RCSB.ORG/PDP/. Structure Explore-1A06

[23] Carter D C; Ho J X. Structure of serum albumin.Adv. Protein Chem.; 1994; 45: 153

[24] Era S; Sogami M. H-NMR and CD studies on the structural transition of serum albumin in the acidic region--the N→F transition. J. Pept. Res.; 1998; 52: 431