onr:"swepub:oai:DiVA.org:umu-13597"
Sökning: onr:"swepub:oai:DiVA.org:umu-13597" > Amide solvent prote...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03517naa a2200349 4500 | |
| 001 | oai:DiVA.org:umu-13597 | |
| 003 | SwePub | |
| 008 | 071012s2007 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-135972 URI |
| 040 | a (SwePub)umu | |
| 041 | a engb engb -1 | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Olofsson, Andersu Umeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten)4 aut0 (Swepub:umu)anol0042 |
| 245 | 1 0 | a Amide solvent protection analysis demonstrates that amyloid-beta(1-40) and amyloid-beta(1-42) form different fibrillar structures under identical conditions. |
| 264 | 1 | c 2007 |
| 338 | a print2 rdacarrier | |
| 520 | a AD (Alzheimer's disease) is a neurodegenerative disorder characterized by self-assembly and amyloid formation of the 39–43 residue long Ab (amyloid-b)-peptide. The most abundant species, Ab(1–40) and Ab(1–42), are both present within senile plaques, but Ab(1–42) peptides are considerably more prone to self-aggregation and are also essential for the development of AD. To understand the molecular and pathological mechanisms behind AD, a detailed knowledge of the amyloid structures of Ab-peptides is vital. In the present study we have used quenched hydrogen/deuterium-exchange NMR experiments to probe the structure of Ab(1–40) fibrils. The fibrils were prepared and analysed identically as in our previous study on Ab(1–42) fibrils, allowing a direct comparison of the two fibrillar structures. The solvent protection pattern of Ab(1–40) fibrils revealed two well-protected regions, consistent with a structural arrangement of two b-strands connected with a bend. This protection pattern partly resembles the pattern found in Ab(1–42) fibrils, but the Ab(1–40) fibrils display a significantly increased protection for the N-terminal residues Phe4–His14, suggesting that additional secondary structure is formed in this region. In contrast, the C-terminal residues Gly37–Val40 show a reduced protection that suggests a loss of secondary structure in this region and an altered filament assembly. The differences between the present study and other similar investigations suggest that subtle variations in fibril-preparation conditions may significantly affect the fibrillar architecture. | |
| 520 | a | |
| 650 | 7 | a NATURVETENSKAPx Biologix Strukturbiologi0 (SwePub)106012 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Structural Biology0 (SwePub)106012 hsv//eng |
| 653 | a NMR | |
| 653 | a Structural biology | |
| 653 | a Strukturbiologi | |
| 700 | 1 | a Lindhagen-Persson, Malinu Umeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Teknisk-naturvetenskaplig fakultet)4 aut |
| 700 | 1 | a Sauer-Eriksson, Elisabethu Umeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Teknisk-naturvetenskaplig fakultet)4 aut0 (Swepub:umu)elsa0002 |
| 700 | 1 | a Öhman, Andersu Umeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Teknisk-naturvetenskaplig fakultet)4 aut0 (Swepub:umu)anoh0004 |
| 710 | 2 | a Umeå universitetb Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten)4 org |
| 773 | 0 | t Biochem Jg 404:1, s. 63-70q 404:1<63-70x 1470-8728 |
| 856 | 4 | u http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=17280549&dopt=Citation |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-13597 |
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