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Post by aqt on Feb 27, 2009 18:21:48 GMT -5
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Post by aqt on Feb 27, 2009 18:22:26 GMT -5
In short, the incredible Bacillus subtilis, which is commonly found in the outside environment rather than in the human intestinal system, continues to benefit mankind ever since its unusual discovery by the Germans in 1941. What's more, it is only one small example of the multitude of "friendly" microorganisms which can create tremendous benefits for humans when ingested, even though they are not necessarily "native" microorganisms to the human body. www.rense.com/general4/bac.htm
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Post by aqt on Feb 27, 2009 18:30:27 GMT -5
: Bacillus subtilis subsp. subtilis str. 168 [BSNR] Model organism for prokaryotic cell differentiation and development Bacteria
Bacillus subtilis. This organism was one of the first bacteria studied, and was named Vibrio subtilis in 1835 and renamed Bacillus subtilis in 1872. It is one of the most well characterized bacterial organisms, and is a model system for cell differentiation and development
www.ncbi.nlm.nih.gov/sites/entrez?db=genomeprj&cmd=Retrieve&dopt=Overview&list_uids=76
Vibrio/ subtilis has quorum sensing ability
subtilis is proposed to use quorum sensing and competence at higher cell density to inherit its own species' DNA. Density-dependent control of competence in ...
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Post by aqt on Feb 27, 2009 18:39:19 GMT -5
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Post by aqt on Feb 28, 2009 20:03:41 GMT -5
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Post by aqt on Feb 28, 2009 20:06:56 GMT -5
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Post by aqt on Feb 28, 2009 20:08:18 GMT -5
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Post by aqt on Feb 28, 2009 20:11:39 GMT -5
Amyloid :: chemical synthesis Three terminally protected short peptides Bis[Boc-D-Leu1-Cys2-OMe] 1, Bis[Boc-Leu1-Cys2-OMe] and Bis[Boc-Val1-Cys2-OMe] 3 exhibit amyloid-like fibrillar morphology. Single crystal X-ray diffraction analysis of peptide 1 clearly demonstrates that it adopts an overall extended backbone molecular conformation that self-assembles to form an intermolecular hydrogen-bonded antiparallel supramolecular beta-sheet structure in crystals. Scanning electron microscopic (SEM) images, transmission electron microscopic (TEM) images and Congo red binding studies vividly demonstrate the amyloid-like fibril formation of peptides 1, 2 and 3. However, after reduction of the disulfide bridge of peptides 1, 2 and 3, three newly generated peptides Boc-D-Leu1-Cys2-OMe 4, Boc-Leu1-Cys2-OMe 5 and Boc-Val1-Cys2-OMe 6 are formed and all of them failed to form any kind of fibril under the same conditions, indicating the important role of the disulfide bond in amyloid-like fibrillogenesis in a peptide model system. lib.bioinfo.pl/meid:29631
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Post by aqt on Feb 28, 2009 20:21:22 GMT -5
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Post by aqt on Mar 1, 2009 20:22:02 GMT -5
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Post by aqt on Mar 2, 2009 13:42:07 GMT -5
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