Research output: Contribution to journal › Article › peer-review
Sup35NMp Morphology Evaluation on Au, Si, Formvar and Mica Surfaces Using AFM, SEM and TEM. / Sokolov, P. A.; Bondarev, S. A.; Belousov, M. V.; Zhouravleva, G. A.; Kasyanenko, N.A.
In: Journal of Structural Biology, Vol. 201, No. 1, 01.2018, p. 5-14.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Sup35NMp Morphology Evaluation on Au, Si, Formvar and Mica Surfaces Using AFM, SEM and TEM
AU - Sokolov, P. A.
AU - Bondarev, S. A.
AU - Belousov, M. V.
AU - Zhouravleva, G. A.
AU - Kasyanenko, N.A.
PY - 2018/1
Y1 - 2018/1
N2 - Prion and some other incurable human neurodegenerative diseases are associated with misfolding of specific proteins, followed by the formation of amyloids. Despite the widespread usage of the transmission electron and of the atomic force microscopy for studing such amyloids, many related methodological issues still have not been studied until now. Here, we consider one of the first amyloids found in Saccharomyces cerevisiae yeast, i.e. Sup35NMp, to study the adsorption of monomeric protein and its fibrils on the surface of mica, silica, gold and on formvar film. Comparison of linear characteristics of these units calculated by processing of images obtained by the atomic force, transmission and scanning electron microscopy was carried out. The minimal number of measurements of fibril diameters to obtain the values in a given confidence interval were determined. We investigated the film formed by monomeric protein on mica surface, which veiled some morphology features of fibrils. Besides, we revealed that parts of the Sup35NMp excluded from the fibril core can form a wide “coat”. The length of the protein forming the core of the fibrils was estimated.
AB - Prion and some other incurable human neurodegenerative diseases are associated with misfolding of specific proteins, followed by the formation of amyloids. Despite the widespread usage of the transmission electron and of the atomic force microscopy for studing such amyloids, many related methodological issues still have not been studied until now. Here, we consider one of the first amyloids found in Saccharomyces cerevisiae yeast, i.e. Sup35NMp, to study the adsorption of monomeric protein and its fibrils on the surface of mica, silica, gold and on formvar film. Comparison of linear characteristics of these units calculated by processing of images obtained by the atomic force, transmission and scanning electron microscopy was carried out. The minimal number of measurements of fibril diameters to obtain the values in a given confidence interval were determined. We investigated the film formed by monomeric protein on mica surface, which veiled some morphology features of fibrils. Besides, we revealed that parts of the Sup35NMp excluded from the fibril core can form a wide “coat”. The length of the protein forming the core of the fibrils was estimated.
KW - Amyloid
KW - Fibril
KW - Microscopy
KW - Prion
KW - Structure
KW - Yeasts
KW - AMYLOID FIBERS
KW - DOMAIN
KW - DETERMINANT
KW - YEAST SUP35
KW - SACCHAROMYCES-CEREVISIAE
KW - SYNUCLEIN STRAINS
KW - ATOMIC-FORCE MICROSCOPY
KW - PRION VARIANTS
KW - BETA-SHEET STRUCTURE
KW - DIVERSITY
UR - http://www.scopus.com/inward/record.url?scp=85032590565&partnerID=8YFLogxK
UR - http://www.mendeley.com/research/sup35nmp-morphology-evaluation-au-si-formvar-mica-surfaces-using-afm-sem-tem
U2 - 10.1016/j.jsb.2017.10.006
DO - 10.1016/j.jsb.2017.10.006
M3 - Article
VL - 201
SP - 5
EP - 14
JO - Journal of Structural Biology
JF - Journal of Structural Biology
SN - 1047-8477
IS - 1
ER -
ID: 7616350