Source 1primary paper1997Proceedings of the National Academy of Sciences
Toolkit/atomic force sensing technique
atomic force sensing technique
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The atomic force sensing technique is an assay method for dynamically probing protein conformational changes with microsecond time resolution. In the cited 1997 study, it was applied to light-induced conformational changes in bacteriorhodopsin.
Usefulness & Problems
Why this is useful
This method is useful for resolving rapid protein conformational dynamics on the microsecond timescale. The available evidence specifically supports its use for monitoring light-triggered structural changes in bacteriorhodopsin.
Source:
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
Source:
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
Problem solved
It addresses the problem of measuring very fast protein conformational changes dynamically rather than only through static structural snapshots. The cited application focuses on primary light-induced events in bacteriorhodopsin.
Source:
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
Problem links
Need precise spatiotemporal control with light input
DerivedThe atomic force sensing technique is an assay method for dynamically probing protein conformational changes with microsecond time resolution. In the cited study, it was applied to light-induced conformational changes in bacteriorhodopsin.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Techniques
Functional AssayTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: sensorswitch architecture: uncaging
The cited application used light as the input modality to induce conformational changes in bacteriorhodopsin. Beyond this, the supplied evidence does not specify construct design, sample preparation, instrumentation parameters, or expression and delivery requirements.
The supplied evidence is limited to a single cited study and one demonstrated application in bacteriorhodopsin. No broader validation across other proteins, quantitative performance benchmarks, or implementation constraints are provided in the evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
time resolution microsecond
Approval Evidence
1 source2 linked approval claimsfirst-pass slug atomic-force-sensing-technique
In this paper a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins.
Source:
applicationsupports
The atomic force sensing technique was applied to light-induced changes in bacteriorhodopsin.
The method is applied to the light-induced changes in the membrane-bound proton pump bacteriorhodopsin (bR).
Source:
method capabilitysupports
The atomic force sensing technique dynamically probes conformational changes in proteins with microsecond time resolution.
a new atomic force sensing technique is presented for dynamically probing conformational changes in proteins. The microsecond time-resolution of the method
Source:
Comparisons
Source-backed strengths
The reported strength is microsecond time resolution for probing protein conformational dynamics. The method was demonstrated in a biologically relevant light-responsive membrane protein, bacteriorhodopsin.
Compared with hydrogen-deuterium exchange coupled to mass spectrometry
atomic force sensing technique and hydrogen-deuterium exchange coupled to mass spectrometry address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: conformational_uncaging; same primary input modality: light
Compared with small-angle X-ray scattering
atomic force sensing technique and small-angle X-ray scattering address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Compared with temperature-dependent FTIR spectroscopy
atomic force sensing technique and temperature-dependent FTIR spectroscopy address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Ranked Citations
- 1.