Secondary Structure Estimation of Proteins Using the Amide III Region of Fourier Transform Infrared Spectroscopy: Application to Analyze Calcium-Binding-Induced Structural Changes in Calsequestrin
暂无分享,去创建一个
Fen-Ni Fu | William R. Trumble | B. Singh | F. Fu | D. Deoliveira | W. Trumble | H. Sarkar | Bal Ram Singh | Hemanta K. Sarkar | Daniel B. Deoliveira | Bal R Singh
[1] D. Wetlaufer,et al. A new basis for interpreting the circular dichroic spectra of proteins. , 1971, Proceedings of the National Academy of Sciences of the United States of America.
[2] H. Susi,et al. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. , 1986, Methods in enzymology.
[3] J. Gomez-Fernandez,et al. Fourier transform infrared spectroscopic studies on the secondary structure of the Ca2+-ATPase of sarcoplasmic reticulum. , 1989, Biochimica et biophysica acta.
[4] E. Ulrich,et al. Detailed analysis of protein structure and function by NMR spectroscopy: survey of resonance assignments. , 1984, Annual review of biophysics and bioengineering.
[5] R. Jakobsen,et al. Infrared Spectra-Structure Correlations and Adsorption Behavior for Helix Proteins , 1990 .
[6] R. Reithmeier,et al. Size and shape of rabbit skeletal muscle calsequestrin. , 1984, The Journal of biological chemistry.
[7] D. Maclennan,et al. Isolation of a calcium-sequestering protein from sarcoplasmic reticulum. , 1971, Proceedings of the National Academy of Sciences of the United States of America.
[8] H. Mantsch,et al. Structure of cytochrome b5 in solution by Fourier-transform infrared spectroscopy. , 1989, Biochemistry.
[9] M. Fuller,et al. Molecular structure of tetanus neurotoxin as revealed by Fourier transform infrared and circular dichroic spectroscopy. , 1990, Biophysical chemistry.
[10] R. Reithmeier,et al. Characterization of skeletal muscle calsequestrin by 1H NMR spectroscopy. , 1984, The Journal of biological chemistry.
[11] R. Williams,et al. Secondary structure of calsequestrin in solutions and in crystals as determined by Raman spectroscopy. , 1986, The Journal of biological chemistry.
[12] M. Fuller,et al. Botulinum neurotoxin type A: Structure and interaction with the micellar concentration of SDS determined by FT-IR spectroscopy , 1991, Journal of protein chemistry.
[13] J. Bandekar,et al. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. , 1986, Advances in protein chemistry.
[14] J. Olinger,et al. Fourier transform infrared studies of ribonuclease in H2O and 2H2O solutions. , 1986, Biochimica et biophysica acta.
[15] P. Carey. CHAPTER 4 – Protein Conformation from Raman and Resonance Raman Spectra , 1982 .
[16] T. Matsui,et al. A Study of the Amide III Band by FT-IR Spectrometry of the Secondary Structure of Albumin, Myoglobin, and γ-Globulin , 1987 .
[17] W. C. Johnson,et al. Secondary structure of proteins through circular dichroism spectroscopy. , 1988, Annual review of biophysics and biophysical chemistry.
[18] H. Mantsch,et al. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. , 1993, Biochemistry.
[19] David C. Lee,et al. Structure of bacteriorhodopsin investigated using Fourier transform infrared spectroscopy and proteolytic digestion , 1987 .
[20] P. Haris,et al. Does Fourier-transform infrared spectroscopy provide useful information on protein structures? , 1992, Trends in biochemical sciences.
[21] A. Dunker,et al. Ca(2+)-induced folding and aggregation of skeletal muscle sarcoplasmic reticulum calsequestrin. The involvement of the trifluoperazine-binding site. , 1993, The Journal of biological chemistry.
[22] G. Petsko,et al. The structure of subtilopeptidase A. I. X-ray crystallographic data. , 1976, Journal of molecular biology.
[23] B. Singh,et al. FT-IR in Combination with the Attenuated Total Reflectance Technique: A Very Sensitive Method for the Structural Analysis of Polypeptides , 1991 .
[24] M. Levitt,et al. Automatic identification of secondary structure in globular proteins. , 1977, Journal of molecular biology.
[25] B. Singh,et al. Fourier Transform Infrared Spectroscopic Analysis of Proteins in Terms of Detectability, Conformation and Surface Adsorption Density , 1992 .
[26] R. Mendelsohn,et al. Thermal denaturation of globular proteins. Fourier transform-infrared studies of the amide III spectral region. , 1987, Biophysical journal.
[27] J. Kraut,et al. Structure of Subtilisin BPN′ at 2.5 Å Resolution , 1969, Nature.
[28] H. Susi,et al. Examination of the secondary structure of proteins by deconvolved FTIR spectra , 1986, Biopolymers.
[29] B. Singh,et al. Structural analysis of botulinum neurotoxin types A and E in aqueous and nonpolar solvents by Fourier transform infrared, second derivative UV absorption, and circular dichroic spectroscopies , 1990, Journal of protein chemistry.
[30] W. Caughey,et al. Protein secondary structures in water from second-derivative amide I infrared spectra. , 1990, Biochemistry.