Post by skyship on Dec 18, 2009 9:42:12 GMT -5
A-beta peptide fibril
click on photo, upclose and personal, folks.
tinyurl.com/ybuxqpl
images.google.com/imgres?imgurl=http://
www.sciencedaily.com/images/2008/05/080512170723-
thumb.jpg&imgrefurl=http://www.sciencedaily.com/releases/
2007/12/071203135744.htm&usg=__3C-FcUCV3VEgg5K_
UrUyDH9u4e0=&h=50&w=46&sz=2&hl=en&start=5&um=1&tb
nid=3O5KwcM_rKP4sM:&tbnh=50&tbnw=46&prev=/images%
3Fq%3Dormation%2Bprocess%2Bof%2Bpeptide-based%2B
nano-assemblies%26hl%3Den%26sa%3DN%26um%3D1
====================================
now compare the one created for nanotech purposes:
where are the biotech experiments, in us?
============================
Abstract
Amyloid fibrils are fibrous polypeptide aggregates that can be formed in vitro and under pathologic conditions, such as in type II diabetes, Alzheimer's and Creutzfeldt-Jakob diseases. Using a range of biophysical techniques including electron microscopy we have analysed the quaternary structure of a mature amyloid fibril formed from the Aβ(1-40) peptide from Alzheimer's disease. We find that the analysed fibril is discernibly polar and represents a left-handed helix consisting of two or three protofilaments. These are organised in a manner so that the cross-section is, under the present resolution conditions (2.6 nm), S-shaped. In the cross-section, each protofilament can accommodate two β-strands, suggesting that each protofilament contains two cross-β-sheets. These data shed new light on the way in which Aβ(1-40) and the protofilaments formed from this peptide are organised within the mature fibril.
Keywords: aggregates; neurodegeneration; protein folding; prion
Abbreviations: 3D, three-dimensional; CEM, cryo-electron microscopy; ss-NMR, solid-state nuclear magnetic resonance
tinyurl.com/ya2o7dp
www.sciencedirect.com/science?_ob=ArticleURL
&_udi=B6WK7-4KPNHTN-1&_user=10&_origUdi=B6TCW-
4NBR3K2-3&_fmt=high&_coverDate=09%2F15%2F2006&_
rdoc=1&_orig=article&_acct=C000050221&_version=1&_
urlVersion=0&_userid=10&md5=16459a4bb15bbf482a807
5b58bc8cd27
skyship
click on photo, upclose and personal, folks.
tinyurl.com/ybuxqpl
images.google.com/imgres?imgurl=http://
www.sciencedaily.com/images/2008/05/080512170723-
thumb.jpg&imgrefurl=http://www.sciencedaily.com/releases/
2007/12/071203135744.htm&usg=__3C-FcUCV3VEgg5K_
UrUyDH9u4e0=&h=50&w=46&sz=2&hl=en&start=5&um=1&tb
nid=3O5KwcM_rKP4sM:&tbnh=50&tbnw=46&prev=/images%
3Fq%3Dormation%2Bprocess%2Bof%2Bpeptide-based%2B
nano-assemblies%26hl%3Den%26sa%3DN%26um%3D1
====================================
now compare the one created for nanotech purposes:
where are the biotech experiments, in us?
============================
Abstract
Amyloid fibrils are fibrous polypeptide aggregates that can be formed in vitro and under pathologic conditions, such as in type II diabetes, Alzheimer's and Creutzfeldt-Jakob diseases. Using a range of biophysical techniques including electron microscopy we have analysed the quaternary structure of a mature amyloid fibril formed from the Aβ(1-40) peptide from Alzheimer's disease. We find that the analysed fibril is discernibly polar and represents a left-handed helix consisting of two or three protofilaments. These are organised in a manner so that the cross-section is, under the present resolution conditions (2.6 nm), S-shaped. In the cross-section, each protofilament can accommodate two β-strands, suggesting that each protofilament contains two cross-β-sheets. These data shed new light on the way in which Aβ(1-40) and the protofilaments formed from this peptide are organised within the mature fibril.
Keywords: aggregates; neurodegeneration; protein folding; prion
Abbreviations: 3D, three-dimensional; CEM, cryo-electron microscopy; ss-NMR, solid-state nuclear magnetic resonance
tinyurl.com/ya2o7dp
www.sciencedirect.com/science?_ob=ArticleURL
&_udi=B6WK7-4KPNHTN-1&_user=10&_origUdi=B6TCW-
4NBR3K2-3&_fmt=high&_coverDate=09%2F15%2F2006&_
rdoc=1&_orig=article&_acct=C000050221&_version=1&_
urlVersion=0&_userid=10&md5=16459a4bb15bbf482a807
5b58bc8cd27
skyship