scholarly journals Redox-induced conformational changes within the Escherichia coli NADH ubiquinone oxidoreductase (complex I): An analysis by mutagenesis and FT-IR spectroscopy

2010 ◽  
Vol 1797 (6-7) ◽  
pp. 659-663 ◽  
Author(s):  
Thorsten Friedrich ◽  
Petra Hellwig
Keyword(s):  
Escherichia Coli ◽  
Ir Spectroscopy ◽  
Conformational Changes ◽  
Complex I ◽  
Ubiquinone Oxidoreductase ◽  
Nadh Ubiquinone Oxidoreductase ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

scholarly journals Differentiation of live, dead and treated cells of Escherichia coli O157:H7 using FT-IR spectroscopy

2012 ◽  
Vol 112 (4) ◽  
pp. 743-751 ◽  
Author(s):  
R. Davis ◽  
A. Deering ◽  
Y. Burgula ◽  
L.J. Mauer ◽  
B.L. Reuhs
Keyword(s):  
Escherichia Coli ◽  
Ir Spectroscopy ◽  
Escherichia Coli O157 ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

Evidence of conformational changes for protein films exposed to high-pressure CO2 by FT-IR spectroscopy

2003 ◽  
Vol 27 (3) ◽  
pp. 283-295 ◽  
Author(s):  
Alberto Striolo ◽  
Alessandro Favaro ◽  
Nicola Elvassore ◽  
Alberto Bertucco ◽  
Vito Di Noto
Keyword(s):  
High Pressure ◽  
Ir Spectroscopy ◽  
Conformational Changes ◽  
Protein Films ◽  
High Pressure Co2 ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

scholarly journals Epicatechin-induced conformational changes in β-lactoglobulin B monitored by FT-IR spectroscopy

SpringerPlus ◽  
2013 ◽  
Vol 2 (1) ◽  
pp. 661 ◽  
Author(s):  
Alessandro Nucara ◽  
Paola Maselli ◽  
Valeria Giliberti ◽  
Marina Carbonaro
Keyword(s):  
Ir Spectroscopy ◽  
Conformational Changes ◽  
Ft Ir ◽  
Β Lactoglobulin ◽  
Ft Ir Spectroscopy

Use of Attenuated Total Reflection—Fourier Transform Infrared Spectroscopy to Measure Collagen Degradation in Historical Parchments

2008 ◽  
Vol 62 (10) ◽  
pp. 1108-1114 ◽  
Author(s):  
Lee Gonzalez ◽  
Tim Wess
Keyword(s):  
Fourier Transform ◽  
Ir Spectroscopy ◽  
Conformational Changes ◽  
Structural Changes ◽  
Fourier Transform Infrared ◽  
Collagen Degradation ◽  
Total Reflection ◽  
Attenuated Total Reflection ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

Developing a noninvasive method to assess the degraded state of historical parchments is essential to providing the best possible care for these documents. The conformational changes observed when collagen molecules, the primary constituent of parchment, unfold have been analyzed using attenuated total reflection–Fourier transform infrared (ATR-FT-IR) spectroscopy and the nanoscopic structural changes have been analyzed using X-ray diffraction (XRD). The relationship between the results obtained from these techniques was studied using principal component analysis, where correlation was found. The extent of gelatinization of historical parchments has been assessed using ATR-FT-IR and XRD and the frequency shifts observed as collagen degrades into gelatin have been reported. These results indicate that collagen degradation can be measured noninvasively in parchment and demonstrate the utility of ATR-FT-IR spectroscopy as a method to investigate historical documents.

scholarly journals Spin labeling of the Escherichia coli NADH ubiquinone oxidoreductase (complex I)

2010 ◽  
Vol 1797 (12) ◽  
pp. 1894-1900 ◽  
Author(s):  
Thomas Pohl ◽  
Thomas Spatzal ◽  
Müge Aksoyoglu ◽  
Erik Schleicher ◽  
Arpad Mihai Rostas ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Complex I ◽  
Spin Labeling ◽  
Ubiquinone Oxidoreductase ◽  
Nadh Ubiquinone Oxidoreductase
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