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Atomic force microscopy differentiates discrete size distributions between membrane protein containing and empty nanolipoprotein particles.
Blanchette, Craig D; Cappuccio, Jenny A; Kuhn, Edward A; Segelke, Brent W; Benner, W Henry; Chromy, Brett A; Coleman, Matthew A; Bench, Graham; Hoeprich, Paul D; Sulchek, Todd A.
Afiliação
  • Blanchette CD; Physical Life Sciences, Lawrence Livermore National Laboratory, Livermore, CA 94551, USA.
Biochim Biophys Acta ; 1788(3): 724-31, 2009 Mar.
Article em En | MEDLINE | ID: mdl-19109924
ABSTRACT
To better understand the incorporation of membrane proteins into discoidal nanolipoprotein particles (NLPs) we have used atomic force microscopy (AFM) to image and analyze NLPs assembled in the presence of bacteriorhodopsin (bR), lipoprotein E4 n-terminal 22k fragment scaffold and DMPC lipid. The self-assembly process produced two distinct NLP populations those containing inserted bR (bR-NLPs) and those that did not (empty-NLPs). The bR-NLPs were distinguishable from empty-NLPs by an average increase in height of 1.0 nm as measured by AFM. Streptavidin binding to biotinylated bR confirmed that the original 1.0 nm height increase corresponds to br-NLP incorporation. AFM and ion mobility spectrometry (IMS) measurements suggest that NLP size did not vary around a single mean but instead there were several subpopulations, which were separated by discrete diameters. Interestingly, when bR was present during assembly the diameter distribution was shifted to larger particles and the larger particles had a greater likelihood of containing bR than smaller particles, suggesting that membrane proteins alter the mechanism of NLP assembly.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bacteriorodopsinas / Lipoproteínas / Proteínas de Membrana Idioma: En Revista: Biochim Biophys Acta Ano de publicação: 2009 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bacteriorodopsinas / Lipoproteínas / Proteínas de Membrana Idioma: En Revista: Biochim Biophys Acta Ano de publicação: 2009 Tipo de documento: Article País de afiliação: Estados Unidos