Biggest discovery: collagen form a long continuous triple helix
[1]
[2]Collagen triple helix[3]
nanophotonics and nanoplasmonics device applications plasmonic solar cells,
Helicity and Filamentation Magnetism—Molder of the Universe[4]
Solar Efficiency by a Third Scientists are always looking for ways to increase the efficiency of renewable energy, and now researchers at the Massachusetts Institute of Technology are utilizing viruses to enhance the efficiency of solar cells at the microscopic level. In an article in the journal Nature Nanotechnology, the scientists revealed that viruses could be used to organize carbon nanotubes in dye-sensitized solar cells, reaping efficiency [5] gains of a full third.
· sospiral "a vent, air hole," from sospirer "breathe," from L. suspirare "breathe deep." spiral, from M.L. spiralis "winding, coiling" (mid-13c.), from L. spira "coil," from Gk. speira "coil, twist, wreath," from PIE *sper- "to turn, twist
· Vrtlog vortex, variant of vertex "an eddy of water, wind, or flame; whirlpool; whirlwind," from stem of vertere "to turn" (see versus). Plural form is vortices. Became prominent in 17c. theories of astrophysics (by Descartes, etc.).
·
http://www.kamlingtrading.com/spiralalgae-eng.htmspiralne alge[6]
Revision Anterior Cruciate Ligament Reconstruction with Doubled Semitendinosus and Gracilis Tendons and Lateral Extra-Articular Reconstruction: Surgical Technique
· sclerosis necrosis cirrhosis scoliosis acidosis apoptosis hypnosis neurosis psychosis apotheosis arteriosus cyanosis meiosis mitosis mononucleosis sarcoidosis diagnosis prognosis fibrosis thrombosis phagocytosis symbiosis amyloidosis aponeurosis arteriosclerosis leukocytosis ptosis halitosis hydronephrosis
Death Spiral
mesopore size is about 5.5–7.5 nm
[7]
plasma membrane get organized Proteins combine into filaments that hug and modify the membrane These proteins wind into helices[8]
[1]
http://archimede.bibl.ulaval.ca/archimede/fichiers/23201/23201003.jpg
[2]
http://alexandria.healthlibrary.ca/documents/notes/bom/unit_1/unit1.images/
35no1.gif
The skin collagens can be divided into various groups based on the structure of their α-chains. First, they can be categorized as homotrimers or heterotrimers. Type III and VII collagens are each homotrimers. Type I and IV collagens are heterotrimers formed from the products of two genes. Type V and VI collagens are heterotrimers formed from the products of three genes.
The collagen types may also be distinguished according to the structure of their collagen molecules (Fig. 2). Types I, III and V collagen form a long continuous triple helix that accounts for most of their length. The other collagen types form triple helices of varying sizes with numerous interruptions, and also possess large non-helical globular domains at one or both ends of the molecules. These features result in types IV, VI and VII collagen forming different aggregate structures to the fibrillar collagens. The interruptions give the collagen molecules flexibility by allowing them to bend, and limit the sites at which lateral interactions can occur. The terminal globular domains limit lateral interactions of the adjacent triple helix, and provide a site at which terminal interactions between collagen molecules can occur
[3]
http://en.wikipedia.org/wiki/Collagen_helix[4] plasmauniverse.info/mag_fields.html
[5]
http://homepages.uwp.edu/pham/bios301/L16stu.pdf
[6]
http://www.marcusrohrerspirulina.com/files/1013/0143/0494/13190079466_ZQ2Cq.jpg
[7] research.ncku.edu.tw/.../e/20080314/5.html
[8]
http://jcb.rupress.org/content/195/5/705
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