Nonaxiality in infrared dichroic ratios of polytopic transmembrane proteins.

[1]  S. Tatulian,et al.  Infrared spectroscopy of proteins and peptides in lipid bilayers , 1997, Quarterly Reviews of Biophysics.

[2]  D. Marsh.  Dichroic ratios in polarized Fourier transform infrared for nonaxial symmetry of beta-sheet structures. , 1997, Biophysical journal.

[3]  R Henderson,et al.  Electron-crystallographic refinement of the structure of bacteriorhodopsin. , 1996, Journal of molecular biology.

[4]  P. Axelsen,et al.  The infrared dichroism of transmembrane helical polypeptides. , 1995, Biophysical journal.

[5]  N. A. Rodionova,et al.  Characterization of two membrane-bound forms of OmpA. , 1995, Biochemistry.

[6]  S. Cowan.  Bacterial porins: lessons from three high-resolution structures: Current Opinion in Structural Biology 1993, 3:501–507 , 1993 .

[7]  P. Lansbury,et al.  Location of .beta.-sheet-forming sequences in amyloid proteins by FTIR , 1991 .

[8]  R. Nazarbaghi,et al.  Isotopically enhanced infrared spectroscopy: a novel method for examining secondary structure at specific sites in conformationally heterogeneous peptides , 1991 .

[9]  R. Garavito,et al.  The orientation of beta-sheets in porin. A polarized Fourier transform infrared spectroscopic investigation. , 1988, Biophysical journal.

[10]  N. Clark,et al.  Polarized infrared spectroscopy of oriented purple membrane. , 1979, Biophysical journal.

[11]  M. Tsubio.  Infrared dichroism and molecular conformation of α‐form poly‐γ‐benzyl‐L‐glutamate , 1962 .