2bfi: Difference between revisions

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[[Image:2bfi.~~gif~~|left|200px]]

[[Image:2bfi.png|left|200px]]

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~~'''~~MOLECULAR BASIS FOR AMYLOID FIBRIL FORMATION AND STABILITY~~'''~~

===MOLECULAR BASIS FOR AMYLOID FIBRIL FORMATION AND STABILITY===

~~==Overview==~~

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The ~~molecular structure of~~ the ~~amyloid fibril has remained elusive because of~~ the ~~difficulty of growing well diffracting crystals~~. ~~By using a sequence-designed polypeptide, we have produced crystals of an amyloid fiber~~. ~~These crystals diffract to high resolution (1 A~~) ~~by electron and x-ray diffraction~~, ~~enabling us to determine a detailed structure for amyloid. The structure reveals that~~ the polypeptides form fibrous crystals composed of antiparallel beta-sheets in a cross-beta arrangement, characteristic of all amyloid fibers, and allows us to determine the side-chain packing within an amyloid fiber. ~~The antiparallel beta~~-~~sheets are zipped together by means of pi~~-bonding between adjacent phenylalanine rings and salt-bridges between charge pairs (glutamic acid-lysine), thus controlling and stabilizing the structure. These interactions are likely to be important in the formation and stability of other amyloid fibrils.

The line below this paragraph, {{ABSTRACT_PUBMED_15630094}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15630094 is the PubMed ID number.

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==About this Structure==

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[[Category: Pi-pi bonding]]

[[Category: X-ray diffraction]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 20~~:13:20 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:36:23 2008''

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-[[Image:2bfi.gif|left|200px]]
+{{Seed}}
+[[Image:2bfi.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2bfi|  PDB=2bfi  |  SCENE=  }}
-'''MOLECULAR BASIS FOR AMYLOID FIBRIL FORMATION AND STABILITY'''
+===MOLECULAR BASIS FOR AMYLOID FIBRIL FORMATION AND STABILITY===
-==Overview==
+<!--
-The molecular structure of the amyloid fibril has remained elusive because of the difficulty of growing well diffracting crystals. By using a sequence-designed polypeptide, we have produced crystals of an amyloid fiber. These crystals diffract to high resolution (1 A) by electron and x-ray diffraction, enabling us to determine a detailed structure for amyloid. The structure reveals that the polypeptides form fibrous crystals composed of antiparallel beta-sheets in a cross-beta arrangement, characteristic of all amyloid fibers, and allows us to determine the side-chain packing within an amyloid fiber. The antiparallel beta-sheets are zipped together by means of pi-bonding between adjacent phenylalanine rings and salt-bridges between charge pairs (glutamic acid-lysine), thus controlling and stabilizing the structure. These interactions are likely to be important in the formation and stability of other amyloid fibrils.
+The line below this paragraph, {{ABSTRACT_PUBMED_15630094}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15630094 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15630094}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Pi-pi bonding]]
 [[Category: X-ray diffraction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:13:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:36:23 2008''