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Spatial structure of heptapeptide Aβ 16-22 (beta-amyloid Aβ 1-40 active fragment) in solution and in complex with a biological membrane model
Kazan (Volga Region) Federal University, Kazan.
Kazan (Volga Region) Federal University, Kazan.
Kazan (Volga Region) Federal University, Kazan.
Luleå tekniska universitet, Institutionen för samhällsbyggnad och naturresurser, Industriell miljö- och processteknik.ORCID-id: 0000-0002-6810-1882
Vise andre og tillknytning
2012 (engelsk)Inngår i: Magnetic Resonance in Chemistry, ISSN 0749-1581, E-ISSN 1097-458X, Vol. 50, nr 12, s. 784-792Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The spatial structure of an active fragment of beta-amyloid Aβ 1-40 heptapeptide Aβ 16-22 (Lys-Leu-Val-Phe-Phe-Ala-Glu) in aqueous buffer solution and in complex with sodium dodecyl sulfate micelles as a model membrane system was investigated by 1H NMR spectroscopy and two-dimensional NMR (TOCSY, HSQC-HECADE (Heteronuclear Couplings from ASSCI-domain experiments with E.COSY-type crosspeaks), NOESY) spectroscopy. Complex formation was confirmed by the chemical shift changes of the heptapeptide's 1H NMR spectra, as well as by the signs and values of the NOE effects in different environments. We compared the spatial structure of the heptapeptide in borate buffer solution and in complex with a model of the cell surface membrane

sted, utgiver, år, opplag, sider
2012. Vol. 50, nr 12, s. 784-792
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URN: urn:nbn:se:ltu:diva-7167DOI: 10.1002/mrc.3880ISI: 000311378700002Scopus ID: 2-s2.0-84869879158Lokal ID: 57de82dc-ee2b-4a40-86df-82c149a8b45cOAI: oai:DiVA.org:ltu-7167DiVA, id: diva2:980055
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Validerad; 2012; 20121010 (andbra)Tilgjengelig fra: 2016-09-29 Laget: 2016-09-29 Sist oppdatert: 2018-07-10bibliografisk kontrollert

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