Hartmann et al., 2015 - Google Patents
Quantification of millisecond protein-folding dynamics in membrane-mimetic environments by single-molecule Forster resonance energy transfer spectroscopyHartmann et al., 2015
- Document ID
- 3940336266459893329
- Author
- Hartmann A
- Krainer G
- Keller S
- Schlierf M
- Publication year
- Publication venue
- Analytical chemistry
External Links
Snippet
An increasing number of membrane proteins in different membrane-mimetic systems have become accessible to reversible unfolding experiments monitored by well-established ensemble techniques. However, only little information is available about kinetic processes …
- 230000012846 protein folding 0 title abstract description 52
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
- G01N33/5008—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
- G01N33/502—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics for testing non-proliferative effects
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N27/00—Investigating or analysing materials by the use of electric, electro-chemical, or magnetic means
- G01N27/26—Investigating or analysing materials by the use of electric, electro-chemical, or magnetic means by investigating electrochemical variables; by using electrolysis or electrophoresis
- G01N27/416—Systems
- G01N27/447—Systems using electrophoresis
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Hartmann et al. | Quantification of millisecond protein-folding dynamics in membrane-mimetic environments by single-molecule Forster resonance energy transfer spectroscopy | |
Nettels et al. | Unfolded protein and peptide dynamics investigated with single-molecule FRET and correlation spectroscopy from picoseconds to seconds | |
Lerner et al. | Toward dynamic structural biology: Two decades of single-molecule Förster resonance energy transfer | |
Dedmon et al. | Mapping long-range interactions in α-synuclein using spin-label NMR and ensemble molecular dynamics simulations | |
Cornish et al. | A survey of single-molecule techniques in chemical biology | |
Keller et al. | Complex RNA folding kinetics revealed by single-molecule FRET and hidden Markov models | |
Chung et al. | Extracting rate coefficients from single-molecule photon trajectories and FRET efficiency histograms for a fast-folding protein | |
Rinas et al. | Development of a microflow system for in-cell footprinting coupled with mass spectrometry | |
Gopich et al. | Single-macromolecule fluorescence resonance energy transfer and free-energy profiles | |
Zhao et al. | Chemiluminescence resonance energy transfer-based detection for microchip electrophoresis | |
Ishii et al. | Two-dimensional fluorescence lifetime correlation spectroscopy. 2. Application | |
Haenni et al. | Intramolecular distances and dynamics from the combined photon statistics of single-molecule FRET and photoinduced electron transfer | |
Li et al. | Same-single-cell analysis for the study of drug efflux modulation of multidrug resistant cells using a microfluidic chip | |
Tsukanov et al. | Conformational dynamics of DNA hairpins at millisecond resolution obtained from analysis of single-molecule FRET histograms | |
Duffy et al. | Determination of electrophoretic mobility distributions through the analysis of individual mitochondrial events by capillary electrophoresis with laser-induced fluorescence detection | |
Neupane et al. | Transition-path probability as a test of reaction-coordinate quality reveals DNA hairpin folding is a one-dimensional diffusive process | |
Nüesch et al. | Single-molecule detection of ultrafast biomolecular dynamics with nanophotonics | |
Slaughter et al. | Single-molecule resonance energy transfer and fluorescence correlation spectroscopy of calmodulin in solution | |
Zhou et al. | Characterization of virus capsids and their assembly intermediates by multicycle resistive-pulse sensing with four pores in series | |
Wu et al. | Combining ultrarapid mixing with photochemical oxidation to probe protein folding | |
Gelot et al. | Ultrafast site-specific fluorescence quenching of 2-aminopurine in a DNA hairpin studied by femtosecond down-conversion | |
Park et al. | Biaxial dielectrophoresis force spectroscopy: A stoichiometric approach for examining intermolecular weak binding interactions | |
Lesoine et al. | Nanochannel-based single molecule recycling | |
Dingfelder et al. | Rapid microfluidic double-jump mixing device for single-molecule spectroscopy | |
Jiang et al. | Microsecond protein folding events revealed by time-resolved fluorescence resonance energy transfer in a microfluidic mixer |