Temperature and hydration dependence of low-frequency spectra of poly-l-glutamic acid with different secondary structures studied by terahertz time-domain spectroscopy

Soft Matter ◽  
2012 ◽  
Vol 8 (6) ◽  
pp. 1997-2006 ◽  
Author(s):  
Naoki Yamamoto ◽  
Ohki Kambara ◽  
Kohji Yamamoto ◽  
Atsuo Tamura ◽  
Shinji Saito ◽  
...  
2011 ◽  
Vol 115 (8) ◽  
pp. 1313-1319 ◽  
Author(s):  
Anjan Chakraborty ◽  
Takashi Inagaki ◽  
Motohiro Banno ◽  
Tomoyuki Mochida ◽  
Keisuke Tominaga

2010 ◽  
Vol 31 (7) ◽  
pp. 799-809 ◽  
Author(s):  
Carlito S. Ponseca ◽  
Ohki Kambara ◽  
Shintaro Kawaguchi ◽  
Kohji Yamamoto ◽  
Keisuke Tominaga

2010 ◽  
Vol 24 (1-2) ◽  
pp. 153-158 ◽  
Author(s):  
Shintaro Kawaguchi ◽  
Ohki Kambara ◽  
Carlito S. Ponseca Jr. ◽  
Mikihiro Shibata ◽  
Hideki Kandori ◽  
...  

By terahertz (THz) time-domain spectroscopy we have measured low-frequency spectra of amino acid (glycine; Gly), short peptides ((Gly)3and (Gly)4), six globular proteins and bacteriorhodopsin (BR). From the analysis of the THz spectra we defined and obtained the reduced absorption cross sections for these cases, which are proportional to the vibrational density of states. We observed anharmonic behaviors in the low-frequency modes of the short peptides. The globular proteins we investigated show a universal feature in the low-frequency spectra. BR shows the dynamical transition in the temperature dependence of the THz spectrum when the sample is hydrated.


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