Physical engineering technology using far-infrared radiation has been gathering attention in chemical, biological, and material research fields. In particular, the high-power radiation at the terahertz region can give remarkable effects on biological materials distinct from a simple thermal treatment. Self-assembly of biological molecules such as amyloid proteins and cellulose fiber plays various roles in medical and biomaterials fields. A common characteristic of those biomolecular aggregates is a sheet-like fibrous structure that is rigid and insoluble in water, and it is often hard to manipulate the stacking conformation without heating, organic solvents, or chemical reagents. We discovered that those fibrous formats can be conformationa...
Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events ...
Far-infrared (FIR) spectroscopy in the spectral region of 50-450 cm -1 was used to study a series of...
Many functionally important structural changes in proteins proceed along the direction of their lowe...
The Author(s) 2012. This article is published with open access at Springerlink.com Abstract Aggregat...
Partially unfolded proteins can self-assemble to form insoluble protein fibrils with diameters in th...
The long range, large scale molecular motions within biological materials are of great interest in m...
Author Institution: Department of Electrical and Computer Engineering, The University of Virginia; U...
AbstractProtein misfolding and aggregation are the hallmark of a number of diseases including Alzhei...
Abstract During the last decades discussions were taking place on the existence of global, non-therm...
Polymerization of monomeric actin into filaments has pivotal roles in cell motility, growth, differe...
© the Owner Societies 2016. Bioinspired fibres and hierarchical nano-materials are based on the self...
Infrared light (IR) was first discovered by Friedrich Wilhelm Herschel in 1800. However, until 1940’...
Our recent experimental research on THz irradiation of actin filaments, which serve as representativ...
Amyloid fibrillation is the root cause of several neuro as well as non-neurological disorders. Under...
Probing molecular systems with light has been critical to deepen our understanding of life sciences....
Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events ...
Far-infrared (FIR) spectroscopy in the spectral region of 50-450 cm -1 was used to study a series of...
Many functionally important structural changes in proteins proceed along the direction of their lowe...
The Author(s) 2012. This article is published with open access at Springerlink.com Abstract Aggregat...
Partially unfolded proteins can self-assemble to form insoluble protein fibrils with diameters in th...
The long range, large scale molecular motions within biological materials are of great interest in m...
Author Institution: Department of Electrical and Computer Engineering, The University of Virginia; U...
AbstractProtein misfolding and aggregation are the hallmark of a number of diseases including Alzhei...
Abstract During the last decades discussions were taking place on the existence of global, non-therm...
Polymerization of monomeric actin into filaments has pivotal roles in cell motility, growth, differe...
© the Owner Societies 2016. Bioinspired fibres and hierarchical nano-materials are based on the self...
Infrared light (IR) was first discovered by Friedrich Wilhelm Herschel in 1800. However, until 1940’...
Our recent experimental research on THz irradiation of actin filaments, which serve as representativ...
Amyloid fibrillation is the root cause of several neuro as well as non-neurological disorders. Under...
Probing molecular systems with light has been critical to deepen our understanding of life sciences....
Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events ...
Far-infrared (FIR) spectroscopy in the spectral region of 50-450 cm -1 was used to study a series of...
Many functionally important structural changes in proteins proceed along the direction of their lowe...