State-of-the-art high-speed atomic force microscopy for investigation of single-molecular dynamics of proteins.
about
Molecular processes studied at a single-molecule level using DNA origami nanostructures and atomic force microscopyFilming biomolecular processes by high-speed atomic force microscopyAtomic force microscopy in biomaterials surface science.DNA switches: from principles to applications.Triple Helix Formation in a Topologically Controlled DNA Nanosystem.Single-molecule observations of RNA-RNA kissing interactions in a DNA nanostructure.Modulating protein-protein interactions: the potential of peptides.Nucleic-Acid-Templated Enzyme Cascades.Single-Molecule Visualization of the Activity of a Zn(2+)-Dependent DNAzyme.Linking two DNA duplexes with a rigid linker for DNA nanotechnology.The Role of Nanomechanics in Healthcare.Single-Molecule Observation of the Photoregulated Conformational Dynamics of DNA Origami Nanoscissors.How We Make DNA Origami.Programmed dissociation of dimer and trimer origami structures by aptamer-ligand complexes.A lock-and-key mechanism for the controllable fabrication of DNA origami structuresSmall molecule binding to a G-hairpin and a G-triplex: a new insight into anticancer drug design targeting G-rich regions
P2860
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P2860
State-of-the-art high-speed atomic force microscopy for investigation of single-molecular dynamics of proteins.
description
2013 nî lūn-bûn
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2013年の論文
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2013年学术文章
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2013年学术文章
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2013年学术文章
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2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
2013年學術文章
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2013年學術文章
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name
State-of-the-art high-speed at ...... olecular dynamics of proteins.
@en
type
label
State-of-the-art high-speed at ...... olecular dynamics of proteins.
@en
prefLabel
State-of-the-art high-speed at ...... olecular dynamics of proteins.
@en
P356
P1433
P1476
State-of-the-art high-speed at ...... olecular dynamics of proteins.
@en
P2093
Hiroshi Sugiyama
P304
P356
10.1021/CR300253X
P577
2013-11-12T00:00:00Z