TY  - JOUR
AU  - Wegmann, Susanne
AU  - Muller, Daniel J
AU  - Mandelkow, Eckhard
TI  - Investigating fibrillar aggregates of Tau protein by atomic force microscopy.
JO  - Methods in molecular biology
VL  - 849
SN  - 1064-3745
CY  - [Heidelberg]
PB  - [Springer]
M1  - DZNE-2020-07506
SN  - 978-1-61779-550-3 (print)
T2  - Methods in Molecular Biology
SP  - 169-183
PY  - 2012
AB  - 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.
KW  - Adsorption
KW  - Aluminum Silicates: chemistry
KW  - Glutaral: chemistry
KW  - Humans
KW  - Microscopy, Atomic Force: methods
KW  - Protein Multimerization
KW  - Protein Structure, Secondary
KW  - Surface Properties
KW  - Time Factors
KW  - tau Proteins: chemistry
KW  - Aluminum Silicates (NLM Chemicals)
KW  - tau Proteins (NLM Chemicals)
KW  - Glutaral (NLM Chemicals)
KW  - mica (NLM Chemicals)
LB  - PUB:(DE-HGF)3 ; PUB:(DE-HGF)16
C6  - pmid:22528090
DO  - DOI:10.1007/978-1-61779-551-0_12
UR  - https://pub.dzne.de/record/141184
ER  -