Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Anomalous amide I infrared absorption of purple membrane.

Literature DB >> 432645

Anomalous amide I infrared absorption of purple membrane.

Abstract

Infrared absorption of purple membrane reveals an amide I frequency that falls outside the range normally found for alpha helices. This may indicate along with x-ray diffraction the existence of bacteriorhodopsin alpha helices with unusual structure.

Entities: Chemical

Mesh：

Substances：

Year: 1979 PMID： 432645 DOI： 10.1126/science.432645

Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728

Keyword Cloud
Cited

15 in total

1. Fourier transform infrared study of the effect of different cations on bacteriorhodopsin protein thermal stability.

Authors: Colin D Heyes; Jianping Wang; Laurie S Sanii; Mostafa A El-Sayed
Journal: Biophys J Date: 2002-03 Impact factor: 4.033

2. What spectroscopy can still tell us about the secondary structure of bacteriorhodopsin.

Authors: R M Glaeser; K H Downing; B K Jap
Journal: Biophys J Date: 1991-04 Impact factor: 4.033

3. Fourier transform infrared evidence for a predominantly alpha-helical structure of the membrane bound channel forming COOH-terminal peptide of colicin E1.

Authors: P Rath; O Bousché; A R Merrill; W A Cramer; K J Rothschild
Journal: Biophys J Date: 1991-03 Impact factor: 4.033

4. The "born energy" problem in bacteriorhodopsin.

Authors: R M Glaeser; B K Jap
Journal: Biophys J Date: 1984-01 Impact factor: 4.033

5. Cell-free co-expression of functional membrane proteins and apolipoprotein, forming soluble nanolipoprotein particles.

Authors: Jenny A Cappuccio; Craig D Blanchette; Todd A Sulchek; Erin S Arroyo; Joel M Kralj; Angela K Hinz; Edward A Kuhn; Brett A Chromy; Brent W Segelke; Kenneth J Rothschild; Julia E Fletcher; Federico Katzen; Todd C Peterson; Wieslaw A Kudlicki; Graham Bench; Paul D Hoeprich; Matthew A Coleman
Journal: Mol Cell Proteomics Date: 2008-07-04 Impact factor: 5.911

Anomalous amide I infrared absorption of purple membrane.

1. Fourier transform infrared study of the effect of different cations on bacteriorhodopsin protein thermal stability.

2. What spectroscopy can still tell us about the secondary structure of bacteriorhodopsin.

3. Fourier transform infrared evidence for a predominantly alpha-helical structure of the membrane bound channel forming COOH-terminal peptide of colicin E1.

4. The "born energy" problem in bacteriorhodopsin.

5. Cell-free co-expression of functional membrane proteins and apolipoprotein, forming soluble nanolipoprotein particles.

6. Evidence for rhodopsin refolding during the decay of Meta II.

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

8. Fourier transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts.

9. Peptide-chain secondary structure of bacteriorhodopsin.

10. Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra.