1hz3

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[[Image:1hz3.gif|left|200px]]
[[Image:1hz3.gif|left|200px]]
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{{Structure
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|PDB= 1hz3 |SIZE=350|CAPTION= <scene name='initialview01'>1hz3</scene>
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The line below this paragraph, containing "STRUCTURE_1hz3", creates the "Structure Box" on the page.
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{{STRUCTURE_1hz3| PDB=1hz3 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hz3 OCA], [http://www.ebi.ac.uk/pdbsum/1hz3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hz3 RCSB]</span>
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'''ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (RESIDUES 10-35)'''
'''ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (RESIDUES 10-35)'''
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==About this Structure==
==About this Structure==
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1HZ3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZ3 OCA].
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1HZ3 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZ3 OCA].
==Reference==
==Reference==
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[[Category: Stimson, E R.]]
[[Category: Stimson, E R.]]
[[Category: Zhang, S.]]
[[Category: Zhang, S.]]
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[[Category: collapsed coil]]
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[[Category: Collapsed coil]]
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[[Category: hydrophobic cluster]]
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[[Category: Hydrophobic cluster]]
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[[Category: hydrophobic patch]]
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[[Category: Hydrophobic patch]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:22:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:12:18 2008''
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Revision as of 16:22, 2 May 2008

Template:STRUCTURE 1hz3

ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (RESIDUES 10-35)


Overview

The self-assembly of the soluble peptide Abeta into Alzheimer's disease amyloid is believed to involve a conformational change. Hence the solution conformation of Abeta is of significant interest. In contrast to studies in other solvents, in water Abeta is collapsed into a compact series of loops, strands, and turns and has no alpha-helical or beta-sheet structure. Conformational stabilization is primarily attributed to van der Waals and electrostatic forces. A large conspicuous uninterrupted hydrophobic patch covers approximately 25% of the surface. The compact coil structure appears meta-stable, and because fibrillization leads to formation of intermolecular beta-sheet secondary structure, a global conformational rearrangement is highly likely. A molecular hypothesis for amyloidosis includes at least two primary driving forces, changes in solvation thermodynamics during formation of amyloid deposits and relief of internal conformational stress within the soluble precursor during formation of lower-energy amyloid fibrils.

About this Structure

1HZ3 is a Single protein structure. Full crystallographic information is available from OCA.

Reference

The Alzheimer's peptide a beta adopts a collapsed coil structure in water., Zhang S, Iwata K, Lachenmann MJ, Peng JW, Li S, Stimson ER, Lu Y, Felix AM, Maggio JE, Lee JP, J Struct Biol. 2000 Jun;130(2-3):130-41. PMID:10940221 Page seeded by OCA on Fri May 2 19:22:57 2008

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