Book/Journal Article

DZNE-2020-07506

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Investigating fibrillar aggregates of Tau protein by atomic force microscopy.

Wegmann, S.Extern* ; Muller, D. J. ; Mandelkow, E. (Last author)DZNE*

2012
[Springer] [Heidelberg]
ISBN: 978-1-61779-550-3 (print), 978-1-61779-551-0 (electronic)

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Please use a persistent id in citations: doi:10.1007/978-1-61779-551-0_12

Abstract: Atomic force microscopy (AFM) has been used in numerous studies to visualize and analyze the structure and conformation of biological samples, from single molecules to biopolymers to cells. The possibility to analyze native samples without fixation, staining and in physiological buffer conditions, combined with the sub-nanometer resolution, makes AFM a versatile tool for the analysis of protein aggregation and amyloid structures. Here, we describe the application of AFM to study fibrillar Tau protein aggregates.

Keyword(s): Adsorption (MeSH) ; Aluminum Silicates: chemistry (MeSH) ; Glutaral: chemistry (MeSH) ; Humans (MeSH) ; Microscopy, Atomic Force: methods (MeSH) ; Protein Multimerization (MeSH) ; Protein Structure, Secondary (MeSH) ; Surface Properties (MeSH) ; Time Factors (MeSH) ; tau Proteins: chemistry (MeSH) ; Aluminum Silicates ; tau Proteins ; Glutaral ; mica

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Contributing Institute(s):

1. Structural Principles of Neurodegeneration (AG (Eckhard) Mandelkow)

Research Program(s):

1. 342 - Disease Mechanisms and Model Systems (POF3-342) (POF3-342)

Appears in the scientific report 2012

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Database coverage:
; NCBI Molecular Biology Database ; SCOPUS

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