Single molecule studies of protein folding using atomic force microscopy.
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Summary
This chapter describes the instrument set-up, the preparation of suitable protein substrate, and the collection of data foromic force microscopy, which is more complex than for conventional stopped-flow ensemble studies, but offer new insights into the function of proteins in vivo.
- Type
- article
- Published
- 2007-01-01
- Cited by
- 12
- References
- 51
- OpenAlex
- https://openalex.org/W16957322
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:24775782
Keywords
Computer science
References
- Biophysical investigations of engineered polyproteins: implications for force data.
- The remarkable mechanical strength of polycystin-1 supports a direct role in mechanotransduction.
- Calibration of atomic force microscope
- Mechanisms of protein folding
- Fingerprinting polysaccharides with single-molecule atomic force microscopy
- Mechanical unfolding intermediates in titin modules
- The molecular elasticity of the extracellular matrix protein tenascin
- Single protein misfolding events captured by atomic force microscopy
- Connectin/titin, giant elastic protein of muscle
- When a module is also a domain: the rôle of the N terminus in the stability and the dynamics of immunoglobulin domains from titin.
- Titins: Giant Proteins in Charge of Muscle Ultrastructure and Elasticity
- The dynamic dialogue between cells and matrices: implications of fibronectin's elasticity.
- Mechanical unfolding of TNfn3: the unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation.
- The mechanical stability of ubiquitin is linkage dependent
- Titin: major myofibrillar components of striated muscle.
- Pathway shifts and thermal softening in temperature-coupled forced unfolding of spectrin domains.
- Oriented binding of the His6-tagged carboxyl-tail of the L-type Ca2+ channel alpha1-subunit to a new NTA-functionalized self-assembled monolayer.
- The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding.
- Calibration of atomic‐force microscope tips
- Dynamic strength of molecular adhesion bonds.
Cited by
- Beyond the native state: Exploring the role of partially folded conformations on the protein energy landscape
- Non-Native Interactions Are Critical for Mechanical Strength in PKD Domains
- Repeat-protein folding: new insights into origins of cooperativity, stability, and topology.
- The folding cooperativity of a protein is controlled by its chain topology
- Spectrin domains lose cooperativity in forced unfolding.
- Spectrin folding versus unfolding reactions and RBC membrane stiffness.
- Protein Folding and Unfolding Under Force
- Conformational dynamics of single protein molecules studied by direct mechanical manipulation.
- Getting the feel of food structure with atomic force microscopy
- Biophysical aspects of biomineralization
- Atomic force microscopy (AFM) and related tools for the imaging of foods and beverages on the nanoscale
- Probe microscopy and photonic force microscopy: principles and applications to food microstructures
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