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. 1995 Jul;69(1):271–273. doi: 10.1016/S0006-3495(95)79898-8

Infrared dichroism of amide I and amide II modes of alpha I- and alpha II-helix segments in membrane proteins.

W C Reisdorf Jr 1, S Krimm 1
PMCID: PMC1236244  PMID: 7669904

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Dwivedi A. M., Krimm S. Vibrational analysis of peptides, polypeptides, and proteins. XVIII. Conformational sensitivity of the alpha-helix spectrum: alpha I- and alpha II-poly(L-alanine). Biopolymers. 1984 May;23(5):923–943. doi: 10.1002/bip.360230509. [DOI] [PubMed] [Google Scholar]
  2. Earnest T. N., Herzfeld J., Rothschild K. J. Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange. Biophys J. 1990 Dec;58(6):1539–1546. doi: 10.1016/S0006-3495(90)82498-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Earnest T. N., Roepe P., Braiman M. S., Gillespie J., Rothschild K. J. Orientation of the bacteriorhodopsin chromophore probed by polarized Fourier transform infrared difference spectroscopy. Biochemistry. 1986 Dec 2;25(24):7793–7798. doi: 10.1021/bi00372a002. [DOI] [PubMed] [Google Scholar]
  4. Glaeser R. M., Downing K. H., Jap B. K. What spectroscopy can still tell us about the secondary structure of bacteriorhodopsin. Biophys J. 1991 Apr;59(4):934–938. doi: 10.1016/S0006-3495(91)82307-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Henderson R., Baldwin J. M., Ceska T. A., Zemlin F., Beckmann E., Downing K. H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol. 1990 Jun 20;213(4):899–929. doi: 10.1016/S0022-2836(05)80271-2. [DOI] [PubMed] [Google Scholar]
  6. Krimm S., Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv Protein Chem. 1986;38:181–364. doi: 10.1016/s0065-3233(08)60528-8. [DOI] [PubMed] [Google Scholar]
  7. Krimm S., Dwivedi A. M. Infrared spectrum of the purple membrane: clue to a proton conduction mechanism? Science. 1982 Apr 23;216(4544):407–408. doi: 10.1126/science.6280277. [DOI] [PubMed] [Google Scholar]
  8. Nabedryk E., Bardin A. M., Breton J. Further characterization of protein secondary structures in purple membrane by circular dichroism and polarized infrared spectroscopies. Biophys J. 1985 Dec;48(6):873–876. doi: 10.1016/S0006-3495(85)83848-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Rothschild K. J., Clark N. A. Anomalous amide I infrared absorption of purple membrane. Science. 1979 Apr 20;204(4390):311–312. doi: 10.1126/science.432645. [DOI] [PubMed] [Google Scholar]
  10. Rothschild K. J., Clark N. A. Polarized infrared spectroscopy of oriented purple membrane. Biophys J. 1979 Mar;25(3):473–487. doi: 10.1016/S0006-3495(79)85317-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Vogel H., Gärtner W. The secondary structure of bacteriorhodopsin determined by Raman and circular dichroism spectroscopy. J Biol Chem. 1987 Aug 25;262(24):11464–11469. [PubMed] [Google Scholar]

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