2bfi

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(New page: 200px<br /><applet load="2bfi" size="350" color="white" frame="true" align="right" spinBox="true" caption="2bfi, resolution 1.1&Aring;" /> '''MOLECULAR BASIS FOR A...)
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==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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[[Category: Atkins, E.]]
[[Category: Atkins, E.]]
[[Category: Johansson, J.]]
[[Category: Johansson, J.]]
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[[Category: Makin, O.Sumner.]]
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[[Category: Makin, O Sumner.]]
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[[Category: Serpell, L.C.]]
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[[Category: Serpell, L C.]]
[[Category: Sikorski, P.]]
[[Category: Sikorski, P.]]
[[Category: amyloid]]
[[Category: amyloid]]
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[[Category: x-ray diffraction]]
[[Category: x-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:23:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:18 2008''

Revision as of 14:37, 21 February 2008


2bfi, resolution 1.1Å

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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.

About this Structure

2BFI is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Molecular basis for amyloid fibril formation and stability., Makin OS, Atkins E, Sikorski P, Johansson J, Serpell LC, Proc Natl Acad Sci U S A. 2005 Jan 11;102(2):315-20. Epub 2005 Jan 3. PMID:15630094

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