Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Scanning electron microscopy as a tool for evaluating morphology of amyloid structures formed on surface plasmon resonance chips
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
Vise andre og tillknytning
2018 (engelsk)Inngår i: Data in Brief, E-ISSN 2352-3409, Vol. 19, s. 1166-1170Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

We demonstrate the use of Scanning Electron microscopy (SEM) in combination with Surface Plasmon Resonance (SPR) to probe and verify the formation of amyloid and its morphology on an SPR chip. SPR is a technique that measures changes in the immobilized weight on the chip surface and is frequently used to probe the formation and biophysical properties of amyloid structures. In this context it is of interest to also monitor the morphology of the formed structures. The SPR chip surface is made of a layer of gold, which represent a suitable material for direct analysis of the surface using SEM. The standard SPR chip used here (CM5-chip, GE Healthcare, Uppsala, Sweden) can easily be disassembled and directly analyzed by SEM. In order to verify the formation of amyloid fibrils in our experimental conditions we analyzed also in-solution produced structures by using Transmission Electron Microscopy (TEM). For further details and experimental findings, please refer to the article published in Journal of Molecular Biology, (Brännström K. et al., 2018) [1].

sted, utgiver, år, opplag, sider
Elsevier, 2018. Vol. 19, s. 1166-1170
HSV kategori
Identifikatorer
URN: urn:nbn:se:umu:diva-149049DOI: 10.1016/j.dib.2018.05.129ISI: 000449869100149PubMedID: 30228999Scopus ID: 2-s2.0-85047834173OAI: oai:DiVA.org:umu-149049DiVA, id: diva2:1218313
Merknad

Refers to: Kristoffer Brännström, Tohidul Islam, Anna L. Gharibyan, Irina Iakovleva, Lina Nilsson, Cheng Choo Lee, Linda Sandblad, Annelie Pamrén, Anders Olofsson. The Properties of Amyloid-β Fibrils Are Determined by their Path of Formation. Journal of Molecular Biology, Volume 430, Issue 13, 22 June 2018, Pages 1940-1949

Tilgjengelig fra: 2018-06-14 Laget: 2018-06-14 Sist oppdatert: 2019-02-04bibliografisk kontrollert

Open Access i DiVA

fulltext(2698 kB)81 nedlastinger
Filinformasjon
Fil FULLTEXT01.pdfFilstørrelse 2698 kBChecksum SHA-512
867d29c4f45626794fa52f338baadcbfeacda1c5537d72abb8b45284fe0e1eefb302dbb4ecddce5055aae233610c0f3ed91b93ab269e916532138da509c74bcf
Type fulltextMimetype application/pdf

Andre lenker

Forlagets fulltekstPubMedScopus

Søk i DiVA

Av forfatter/redaktør
Brännström, KristofferGharibyan, Anna L.Islam, TohidulIakovleva, IrinaNilsson, LinaLee, Cheng ChooSandblad, LindaPamrén, AnnelieOlofsson, Anders
Av organisasjonen
I samme tidsskrift
Data in Brief

Søk utenfor DiVA

GoogleGoogle Scholar
Totalt: 81 nedlastinger
Antall nedlastinger er summen av alle nedlastinger av alle fulltekster. Det kan for eksempel være tidligere versjoner som er ikke lenger tilgjengelige

doi
pubmed
urn-nbn

Altmetric

doi
pubmed
urn-nbn
Totalt: 599 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf