Michael Ding: Difference between revisions

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Terahertz (THz) Spectroscopy is an emerging technology that will become a useful tool for numerous aspects of physical chemistry. In terms of frequency, THz spectroscopy covers the region from ~0.1 THz to 10 THz, which lies in the border between far infrared and microwave.  Due to the nature of THz radiation, the spectra represent information on intermolecular vibration as well as the translations and liberation of the molecule. Driven by the foreseeable applications, the knowledge of THz Spectroscopy had been greatly expanded over the last few years.
Terahertz (THz) Spectroscopy is an emerging technology that will become a useful tool for numerous aspects of physical chemistry. In terms of frequency, THz spectroscopy covers the region from ~0.1 THz to 10 THz, which lies in the border between far infrared and microwave.  Due to the nature of THz radiation, the spectra represent information on intermolecular vibration as well as the translations and liberation of the molecule. Driven by the foreseeable applications, the knowledge of THz Spectroscopy had been greatly expanded over the last few years.


 
[[Fibril Forming Peptide]]
==Terahertz spectroscopy on fibril forming peptide==
==Terahertz spectroscopy on fibril forming peptide==
A) related articles:  
A) related articles:  

Revision as of 07:10, 23 January 2008

Terahertz spectroscopy - Intro

Terahertz (THz) Spectroscopy is an emerging technology that will become a useful tool for numerous aspects of physical chemistry. In terms of frequency, THz spectroscopy covers the region from ~0.1 THz to 10 THz, which lies in the border between far infrared and microwave. Due to the nature of THz radiation, the spectra represent information on intermolecular vibration as well as the translations and liberation of the molecule. Driven by the foreseeable applications, the knowledge of THz Spectroscopy had been greatly expanded over the last few years.

Fibril Forming Peptide

Terahertz spectroscopy on fibril forming peptide

A) related articles:

1. The first crystal of fragments of yeast prion: File:Structure of the cross- spine of amyloid-like fibrils.pdf.

The second paper come out on Ribonuclease A: File:Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.pdf

2. experimental procedure: File:An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid.pdf

3. follow up studies had identified 8 classes of zipper structure. File:Atomic structures of amyloid cross-b.pdf





Project source: Literature