Quantitation of secondary structure in ATR infrared spectroscopy

Biophysical Journal

Volumn 77, Issue 5, 1999, Pages 2630-2637

  Marsh, Derek ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

LIPOCORTIN 5; PHOSPHATIDYLCHOLINE;

ABSORPTION SPECTROSCOPY; ARTICLE; GEOMETRY; INFRARED RADIATION; INFRARED SPECTROSCOPY; MEMBRANE VESICLE; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SPECTROSCOPY;

EID: 0032734050     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77096-7     Document Type: Article

References (36)

1. Arkin, I. T., M. Rothmann, C. F. C. Ludlam, S. Aimoto, D. M. Engelman, K. J. Rothschild, and S. O. Smith. 1995. Structural model of the phospholamban ion channel complex in phospholipid membranes. J. Mol. Biol. 248:824-834.
2. Arkin, I. T., W. P. Russ, M. Lebendiker, and S. Schuldiner. 1996. Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle. Biochemistry. 35:7233-7238.
3. Bechinger, B., J. M. Ruysschaert, and E. Goormaghtigh. 1999. Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra. Biophys. J. 76:552-563.
4. Cabiaux, V., R. Brasseur, R. Wattiez, P. Falmagne, J.-M. Ruysschaert, and E. Goormaghtigh. 1989. Secondary structure of diphtheria toxin and its fragments interacting with acidic liposomes studied by polarized infrared spectroscopy. J. Biol. Chem. 264:4928-4938.
5. Chirgadze, Y. N., B. V. Shestopalov, and S. Y. Venyaminov. 1973. Intensities and other spectral parameters of infrared amide bands of polypeptides in the β- and random forms. Biopolymers. 12:1337-1351.
6. Chirgadze, Y. N., and E. V. Brazhnikov. 1974. Intensities and other spectral parameters of infrared amide bands of polypeptides in the α-helical form. Biopolymers. 13:1701-1712.
7. Citra, M. J., and P. H. Axelsen. 1996. Determination of molecular order in supported lipid membranes by internal reflection Fourier transform infrared spectroscopy. Biophys. J. 71:1796-1805.
8. de Jongh, H. H. J., E. Goormaghtigh, and J.-M. Ruysschaert. 1996. The different molar absorptivities of the secondary structure types in the amide I region: an attenuated total reflection infrared study on globular proteins. Anal. Biochem. 242:95-103.
9. Duda, G., A. J. Schouten, T. Arndt, G. Lieser, G. F. Schmidt, C. Bubeck, and G. Wegner. 1988. Preparation and characterization of monolayers and multilayers of preformed polymers. Thin Solid Films. 159:221-230.
10. Fringeli, U. P. 1980. Distribution and diffusion of alamethicin in a lecithin/ water model membrane system. J. Membrane Biol. 54:203-212.
11. Fringeli, U. P. 1992. In situ infrared attenuated total reflection (IR ATR) spectroscopy: a complementary analytical tool for drug design and drug delivery. Chimia. 46:200-214.
12. Fringeli, U. P. 1993. In situ infrared attenuated total reflection membrane spectroscopy. In Internal Reflection Spectroscopy: Theory and Application. Practical Spectroscopy Series, Vol. 14. F. M. Mirabella Jr., editor. Marcel Dekker, New York. 255-324.
13. Fringeli, U. P., and H. H. Günthard. 1981. Infrared membrane spectroscopy. In Membrane Spectroscopy. Molecular Biology Biochemistry and Biophysics, Vol. 31. E. Grell, editor. Springer-Verlag, Berlin/Heidelberg. 270-332.
14. Goormaghtigh, E., V. Cabiaux, and J.-M. Ruysschaert. 1990. Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. Eur. J. Biochem. 193:409-420.
15. Gray, C., S. A. Tatulian, S. A. Wharton, and L. K. Tamm. 1996. Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of influenza hemagglutinin fusion peptide with lipid bilayers. Biophys. J. 70:2275-2286.
16. Gremlich, H. U., U. P. Fringeli, and R. Schwyzer. 1983. Conformational changes of adrenocorticotropin peptides upon interaction with lipid membranes revealed by infrared attenuated total reflection spectroscopy. Biochemistry. 22:4257-4264.
17. Harrick, N. J. 1967. Internal Reflection Spectroscopy. Wiley, New York.
18. Lüneberg, J., I. Martin, F. Nüssler, J.-M. Ruysschaert, and A. Herrmann. 1995. Structure and topology of the influenza virus fusion peptide in lipid bilayers. J. Biol. Chem. 270:27606-27614.
19. Marsh, D. 1997. Dichroic ratios in polarized Fourier transform infrared for nonaxial symmetry of β-sheet structures. Biophys. J. 72:2710-2718.
20. Marsh, D. 1998. Nonaxiality in infrared dichroic ratios of polytopic transmembrane proteins. Biophys. J. 75:354-358.
21. Marsh, D. 1999. Spin label ESR spectroscopy and FTIR spectroscopy for structural/dynamic measurements on ion channels. Methods Enzymol. 294(C):59-92.
22. Picard, F., T. Buffeteau, B. Desbat, M. Auger, and M. Pezolet. 1999. Quantitative orientation measurements in thin lipid films by attenuated total reflection infrared spectroscopy. Biophys. J. 76:539-551.
23. Rodionova, N. A., S. A. Tatulian, R. Surrey, F. Jähnig, and L. K. Tamm. 1995. Characterization of two membrane-bound forms of OmpA. Biochemistry. 34:1921-1929.
24. +-ATPase and of its membrane-associated proteolytic peptides. J. Biol. Chem. 272:262-270.
25. Raussens, V., C. A. Fisher, E. Goormaghtigh, R. O. Ryan, and J.-M. Ruysschaert. 1998. The low density lipoprotein receptor active conformation of apolipoprotein E. Helix organization in N-terminal domain-phospholipid disc particles. J. Biol. Chem. 273:25825-25830.
26. Schmitt, F.-J., and M. Müller. 1997. Conformation and orientation analysis of modified polyglutamates in thin films by ATR infrared spectroscopy. Thin Solid Films. 310:138-147.
27. Silvestro, L., and P. H. Axelsen. 1999. Fourier transform infrared linked analysis of conformational changes in annexin V upon membrane binding. Biochemistry. 38:113-121.
28. Suzuki, E. 1967. A quantitative study of the amide vibrations in the infra-red spectrum of silk fibroin. Spectrochim. Acta. 23A:2303-2308.
29. Tamm, L. K., and S. A. Tatulian. 1993. Orientation of functional and nonfunctional PTS permease signal sequences in lipid bilayers. A polarized attenuated total reflection infrared study. Biochemistry. 32: 7720-7726.
30. Tamm, L. K., and S. A. Tatulian. 1997. Infrared spectroscopy of proteins and peptides in lipid bilayers. Q. Rev. Biophys. 30:365-429.
31. Tatulian, S. A., P. Hinterdorfer, G. Baber, and L. K. Tamm. 1995a. Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy. EMBO J. 14:5514-5523.
32. Tatulian, S. A., L. R. Jones, L. G. Reddy, D. L. Stokes, and L. K. Tamm. 1995b. Secondary structure and orientation of phospholamban reconstituted in supported bilayers from polarized attenuated total reflection FTIR spectroscopy. Biochemistry. 34:4448-4456.
33. 2 induced by membrane binding: a clue to interfacial activation? J. Mol. Biol. 268:809-815.
34. + channel (SKC1): secondary structure characterization from FTIR spectroscopy. FEBS Lett. 423:205-212.
35. 2O) solutions. I. Spectral parameters of amino acid residue absorption bands. Biopolymers. 30: 1243-1257.
36. 2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in α-, β-, and random coil conformations. Biopolymers. 30:1259-1271.