1hz3: Difference between revisions

Revision as of 10:09, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1hz3.png

Template:STRUCTURE 1hz3

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

Template:ABSTRACT PUBMED 10940221

About this StructureAbout this Structure

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

ReferenceReference

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 Tue Jul 1 10:09:34 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1hz3.gif|left|200px]]
+{{Seed}}
+[[Image:1hz3.png|left|200px]]
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 {{STRUCTURE_1hz3|  PDB=1hz3  |  SCENE=  }}
-'''ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (RESIDUES 10-35)'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10940221}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10940221 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10940221}}
 ==About this Structure==
-HZ3 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZ3 OCA].
+HZ3 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZ3 OCA].
 ==Reference==
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 [[Category: Hydrophobic cluster]]
 [[Category: Hydrophobic patch]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:22:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 10:09:34 2008''