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  • Baumruk V, Huo D, Dukor RK, Keiderling TA, LeLeivre D, Brack A. 1994. Conformational study of sequential Lys-Leu based polymers and oligomers using vibrational and electronic circular dichroism spectra. Biopoly-mers 34: 11151121.
  • Baumruk V, Keiderling TA. 1993. Vibrational circular dichroism of proteins in H2O solution. J Am Chem Soc 115: 69396942.
  • Berjot M, Marx J, Alix AJP. 1987. Determination of the secondary structure of proteins from the Raman amide I band: The reference intensity profiles method. J Raman Spectrosc 18: 289300.
  • Bitto E. 1993. Study of protein conformation by mathematical analysis of spectroscopic data [thesis]. Prague: Charles University.
  • Brahms S, Brahms J. 1980. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J Mol Biol 138: 149178.
  • Bussian BM, Sander C. 1989. How to determine protein secondary structure in solution by Raman spectroscopy: Practical guide and test case DNase I. Biochemistry 28: 42714277.
  • Byler DM, Susi H. 1986. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25: 469487.
  • Chang CT, Wu CSC, Yang JT. 1978. Circular dichroic analysis of protein conformation: Inclusion of the β–turns. Anal Biochem 91: 1331.
  • Chen YH, Yang JT. 1971. Secondary structure of proteins by circular dichroism. Biochem Biophys Res Commun 44: 12851291.
  • Chen YH, Yang JT, Martinez HM. 1972. Determination of the secondary structure of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11: 41204131.
  • Compton LA, Johnson WC Jr. 1986. Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal Biochem 155: 155167.
  • Dousseau F, Pezolet M. 1990. Determination of the secondary structure content of protein in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods. Biochemistry 29: 87718779.
  • Dukor RK, Keiderling TA. 1991. Reassessment of the random coil conformation. Vibrational circular dichroism study of proline oligopeptides and related polypeptides. Biopolymers 31: 17471761.
  • Dukor RK, Pancoska P, Prestrelski S, Arakawa T, Keiderling TA. 1992. Comparison of FTIR and vibrational circular dichroism results for two protein hormones. Implications regarding secondary structure. Arch Biochem Biophys 298: 678681.
  • Freedman TB, Nafie LA, Keiderling TA. 1995. Vibrational optical activity of oligopeptides. Biopolymers (Pept Sci) 37. SForthcoming.
  • Greenfield N, Fasman GD. 1969. Computed circular dichroism spectra for evaluation of protein conformation. Biochemistry 8: 41084116.
  • Grishina IB, Woody RW. 1995. Contribution of tryptophan side chains to the circular dichroism of globular proteins: Exciton couplets and coupled oscillators. Faraday Discuss Chem Soc 99. Forthcoming.
  • Gupta VP, Keiderling TA. 1992. Vibrational circular dichroism of the amide II band of proteins and model polypeptides in H2O. Biopolymers 32: 239248.
  • Hennessey JP Jr., Johnson WC Jr. 1981. Information content in the circular dichroism of proteins. Biochemistry 20: 10851094.
  • Johnson WC Jr. 1985. Circular dichroism and its empirical application to biopolymers. Methods Biochem Anal 31: 61163.
  • Johnson WC Jr. 1988. Secondary structure of proteins through circular dichroism spectroscopy. Annu Rev Biophys Chem 17: 145166.
  • Johnson WC Jr. 1990. Protein secondary structure and circular dichroism: A practical guide. Proteins Struct Fund Genet 7: 205214.
  • Kabsch W, Sander C. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 25772637.
  • Keiderling TA. 1981. Vibrational circular dichroism. Appl Spectrosc Rev 17: 189226.
  • Keiderling TA. 1990. Vibrational circular dichroism comparison of technique and practical considerations. In: FerraroJR, KrishnanK, eds. Practical Fourier transform infrared spectroscopy industrial and laboratory chemical analyses. San Diego, California: Academic Press, pp 203284.
  • Keiderling TA. 1993. Vibrational circular dichroism of proteins, polysaccharides, and nucleic acids. In: BaianuIC, PessenH, KumosinskiTF, eds. Physical chemistry of food processes, advanced techniques, structures, and applications. New York: van Nostrand Reinhold. pp 307337.
  • Keiderling TA. 1994. Vibrational circular dichroism spectroscopy of peptides and proteins. In: NakanishiK, BerovaN, WoodyRW, eds. Circular dichroism principles and applications. New York: VCH Publishers, pp 497521.
  • Keiderling TA, Pancoska P. 1993. Structural studies of macromolecules using vibrational circular dichroism. In: ClarkRJH, HesterRE, eds. Biomolecular spectroscopy, part B. Chichester, UK: Wiley, pp 267315.
  • Keiderling TA, Wang B, Urbanova M, Pancoska P, Dukor RK. 1995. Empirical studies of protein secondary structure by vibrational circular dichroism and related techniques: α–Lactalbumin and lysozyme examples. Faraday Discuss Chem Soc 99. Forthcoming.
  • Keiderling TA, Yasui SC, Dukor RK, Yang L. 1989. Application of vibrational circular dichroism to synthetic polypeptides and polynucleic acids. Polymer Preprints 30: 423424.
  • LaBrake CC, Wang L, Keiderling TA, Fung LWM. 1993. Fourier transform infrared spectroscopic studies of the secondary structure of spectrin under different ionic strengths. Biochemistry 32: 1029610302.
  • Lee DC, Haris PI, Chapman D, Mitchell RC. 1990. Determination of protein secondary structure using factor analysis of infrared spectra. Biochemistry 29: 91859193.
  • Levitt M, Chothia C. 1976. Structural patterns in globular proteins. Nature 261: 552558.
  • Levitt M, Greer J. 1977. Automatic identification of secondary structures in globular proteins. J Mol Biol 114: 181239.
  • Malinowski ER, Howery DG. 1980. Factor analysis in chemistry. New York: Wiley.
  • Manavalan P, Johnson WC Jr. 1987. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal Biochem 167: 7685.
  • Manning M. 1989. Underlying assumptions in the estimation of secondary structure content in proteins by circular dichroism spectroscopy — A critical review. J Pharmaceut Biomed Anal 7: 11031119.
  • Manning M, Sreerama N, Woody RW. 1992. Improved models for tyrosine and phenylalanine contributions to the protein circular dichroism spectra. Biophys J 61: A347.
  • Manning M, Woody RW. 1989. Theoretical circular dichroism studies of polypeptide helices: Examination of important electronic and geometric factors. Biopolymers 31: 561586.
  • Mantsch HH, Casal HL, Jones RN. 1986. Resolution enhancement of infrared spectra of biological systems. In: ClarkRJH, HesterRE, eds. Biomolecular spectroscopy, vol 13. London: Wiley & Sons, pp 146.
  • Pancoska P, Bitto E, Janota V, Keiderling TA. 1995. Quantitative analysis of vibrational circular dichroism spectra of proteins. Problems and perspectives. Faraday Discuss Chem Soc 99. Forthcoming.
  • Pancoska P, Blazek M, Keiderling TA. 1992. Relationships between secondary structure fractions for globular proteins. Neural network analyses of crystallographic data sets. Biochemistry 31: 1025010257.
  • Pancoska P, Fric I, Blaha K. 1979. Modified factor analysis of the circular dichroism spectra, applied to a series of cyclodipeptides containing L-proline. Collect Czech Chem Commun 44: 12961312.
  • Pancoska P, Keiderling TA. 1991. Systematic comparison of statistical analyses of electronic and vibrational circular dichroism for secondary structure prediction of selected proteins. Biochemistry 30: 68856895.
  • Pancoska P, Wang L, Keiderling TA. 1993. Comparison of protein FTIR absorption and vibrational circular dichroism. VCD frequency analyses in terms of secondary structure. Protein Sci 2: 411419.
  • Pancoska P, Yasui SC, Keiderling TA. 1989. Enhanced sensitivity to conformation in various proteins. Vibrational circular dichroism results. Biochemistry 28: 59175923.
  • Pancoska P, Yasui SC, Keiderling TA. 1991. Statistical analyses of the vibrational circular dichroism of selected proteins and relationship to secondary structures. Biochemistry 30: 50895103.
  • Perczel A, Hollosi M, Tusnady G, Fasman GD. 1991. Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins. Protein Eng 4: 669679.
  • Press WH. 1992. Numerical recipes in C:The art of scientific computing, 2nd ed, version 20. New York: Cambridge University Press.
  • Pribic R, van Stokkum IHM, Chapman D, Haris PI, Bloemendal M. 1993. Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra. Anal Biochem 214: 366378.
  • Provencher SW, Glöckner J. 1981. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20: 3337.
  • Sarver RW, Krueger WC. 1991a. Protein secondary structure from Fourier transform infrared spectroscopy. Anal Biochem 194: 89100.
  • Sarver RW, Krueger WC. 1991b. An infrared and circular dichroism combined approach to the analysis of protein secondary structure. Anal Biochem 199: 6167.
  • Sen AC, Keiderling TA. 1984. Vibrational circular dichroism of polypeptides II. Solution amide II and deuteration results. Biopolymers 23: 15191532.
  • Sharaf MA, Illman DL, Kowalski BR. 1986. Chemometrics. New York: John Wiley.
  • Siegel JB, Steinmetz WE, Long GL. 1980. A computer assisted model for estimating protein secondary structure from circular dichroism spectra: Comparison of animal lactate dehydrogenases. Anal Biochem 104: 160167.
  • Sreerama N, Woody RW. 1993. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem 209: 3244.
  • Sreerama N, Woody RW. 1994. Protein secondary structure from circular dichroism spectroscopy — Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods. J Mol Biol 242: 497507.
  • Toniolo C, Crisma M, Bonora GM, Klajc B, Lelj F, Grimaldi P, Rosa A, Polinelli S, Boesten WHJ, Meijer EM, Schoemaker HE, Kamphuis J. 1991. Structure of peptides from α–amino acids methylated at the α–carbon. Int J Pept Protein Res 38: 242256.
  • Toumadje A, Alcorn SW, Johnson WC Jr. 1992. Extending CD spectra of proteins to 168 nm improves the analysis for secondary structures. Anal Biochem 200: 321331.
  • Urbanova M, Pancoska P, Keiderling TA. 1993. Spectroscopic study of the temperature-dependent conformation of glucoamylase. Biochim Biophys Acta 1203: 290294.
  • van Stokkum IHM, Spoelder HJW, Bloemendal M, van Grundelle R, Groen FCA. 1990. Estimation of protein secondary structure and error analysis from circular dichroism spectra. Anal Biochem 191: 110118.
  • Venyaminov SYu, Kalnin NN. 1990. Quantitative infrared spectroscopy of peptide compounds in water (H2O) III: Estimation of the protein secondary structure. Biopolymers 30: 12731280.
  • Williams RW. 1986. Protein secondary structure analysis using Raman amide I and amide III spectra. Methods Enzymol 130: 311331.
  • Yang JT, Wu CSC, Martinez HM. 1986. Calculation of protein conformation from circular dichroism spectra. Methods Enzymol 130: 208269.
  • Yasui SC, Keiderling TA. 1986. Vibrational circular dichroism of polypeptides VII. Film and solution studies of B-forming homo-oligopeptides. J Am Chem Soc 108: 55765581.
  • Yasui SC, Keiderling TA, Bonora GM, Toniolo C. 1986a. Vibrational circular dichroism of polypeptides V. A study of 310 helical octapeptides. Biopolymers 25: 7989.
  • Yasui SC, Keiderling TA, Formaggio F, Bonora GM, Toniolo C. 1986b. Thermolysis of 1R,2R–1,2-dideuteriocyclobutane. An application of vibrational circular dichroism to kinetic analysis. J Am Chem Soc 108: 49884993.
  • Yoder G, Keiderling TA, Crisma M, Formaggio F, Toniolo C. 1995. Characterization of β–bend ribbon spiral forming peptides using electronic and vibrational circular dichroism. Biopolymers 35: 103111.