Source 1primary paper2002Biochemistry
Toolkit/small-angle X-ray scattering
small-angle X-ray scattering
Also known as: SAXS
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Small-angle X-ray scattering (SAXS) is a structural characterization assay used to directly observe solution-state conformational changes in light-responsive proteins. In the cited phototropin literature, SAXS was used with other biophysical approaches to study multidomain phototropins from Chlamydomonas and Arabidopsis.
Usefulness & Problems
Why this is useful
SAXS is useful for probing global protein architecture and conformational change in solution when high-resolution structural information is difficult to obtain. In the cited context, it supported investigation of blue-light-responsive phototropins, which are light-activated kinases relevant to plant signaling and optogenetic tool inspiration.
Source:
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
Problem solved
This assay helps address the difficulty of obtaining structural information on multidomain phototropins under solution conditions. It provides direct observation of light-associated conformational changes where high-resolution structures remain challenging.
Problem links
Need conditional control of signaling activity
DerivedSmall-angle X-ray scattering (SAXS) is a structural characterization assay used to directly observe solution-state conformational changes in light-responsive proteins. In the cited phototropin literature, SAXS supported models of multidomain phototropins from Chlamydomonas and Arabidopsis with an extended linear domain arrangement and LOV2-kinase N-lobe contact.
Need precise spatiotemporal control with light input
DerivedSmall-angle X-ray scattering (SAXS) is a structural characterization assay used to directly observe solution-state conformational changes in light-responsive proteins. In the cited phototropin literature, SAXS supported models of multidomain phototropins from Chlamydomonas and Arabidopsis with an extended linear domain arrangement and LOV2-kinase N-lobe contact.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
conformational change detectionconformational uncagingConformational Uncagingstructural characterizationstructural characterizationTarget processes
signalingInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: sensorswitch architecture: uncaging
The available evidence supports use of SAXS as a solution-state biophysical assay applied to multidomain phototropins from Chlamydomonas and Arabidopsis. No specific beamline setup, sample preparation requirements, illumination protocol, or construct design details are provided in the supplied evidence.
The evidence does not provide quantitative performance metrics, resolution limits, or detailed experimental conditions for the SAXS measurements. The cited review also states that high-resolution structural information on phototropins remains challenging to obtain, indicating that SAXS does not by itself resolve that gap.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2review2021Journal of Biological Chemistry
Ranked Claims
Phototropins contain two blue-light-sensing LOV domains, LOV1 and LOV2, together with a C-terminal serine/threonine kinase domain.
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase.
Phototropins contain two blue-light-sensing LOV domains, LOV1 and LOV2, together with a C-terminal serine/threonine kinase domain.
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase.
Phototropins contain two blue-light-sensing LOV domains, LOV1 and LOV2, together with a C-terminal serine/threonine kinase domain.
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase.
Phototropins contain two blue-light-sensing LOV domains, LOV1 and LOV2, together with a C-terminal serine/threonine kinase domain.
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase.
Phototropins contain two blue-light-sensing LOV domains, LOV1 and LOV2, together with a C-terminal serine/threonine kinase domain.
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase.
Phototropins contain two blue-light-sensing LOV domains, LOV1 and LOV2, together with a C-terminal serine/threonine kinase domain.
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase.
Phototropins contain two blue-light-sensing LOV domains, LOV1 and LOV2, together with a C-terminal serine/threonine kinase domain.
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase.
Phototropins contain two blue-light-sensing LOV domains, LOV1 and LOV2, together with a C-terminal serine/threonine kinase domain.
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase.
Phototropins contain two blue-light-sensing LOV domains, LOV1 and LOV2, together with a C-terminal serine/threonine kinase domain.
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase.
Phototropins contain two blue-light-sensing LOV domains, LOV1 and LOV2, together with a C-terminal serine/threonine kinase domain.
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase.
Phototropins are light-activated kinases important for plant physiology and have inspired diverse optogenetic tools.
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
Phototropins are light-activated kinases important for plant physiology and have inspired diverse optogenetic tools.
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
Phototropins are light-activated kinases important for plant physiology and have inspired diverse optogenetic tools.
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
Phototropins are light-activated kinases important for plant physiology and have inspired diverse optogenetic tools.
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
Phototropins are light-activated kinases important for plant physiology and have inspired diverse optogenetic tools.
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
Phototropins are light-activated kinases important for plant physiology and have inspired diverse optogenetic tools.
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
Phototropins are light-activated kinases important for plant physiology and have inspired diverse optogenetic tools.
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
Phototropins are light-activated kinases important for plant physiology and have inspired diverse optogenetic tools.
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
Phototropins are light-activated kinases important for plant physiology and have inspired diverse optogenetic tools.
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
Phototropins are light-activated kinases important for plant physiology and have inspired diverse optogenetic tools.
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
High-resolution structural information on phototropins remains challenging to obtain and is presented as important for both fundamental understanding and engineering efforts.
the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.
High-resolution structural information on phototropins remains challenging to obtain and is presented as important for both fundamental understanding and engineering efforts.
the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.
High-resolution structural information on phototropins remains challenging to obtain and is presented as important for both fundamental understanding and engineering efforts.
the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.
High-resolution structural information on phototropins remains challenging to obtain and is presented as important for both fundamental understanding and engineering efforts.
the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.
High-resolution structural information on phototropins remains challenging to obtain and is presented as important for both fundamental understanding and engineering efforts.
the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.
High-resolution structural information on phototropins remains challenging to obtain and is presented as important for both fundamental understanding and engineering efforts.
the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.
High-resolution structural information on phototropins remains challenging to obtain and is presented as important for both fundamental understanding and engineering efforts.
the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.
High-resolution structural information on phototropins remains challenging to obtain and is presented as important for both fundamental understanding and engineering efforts.
the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.
High-resolution structural information on phototropins remains challenging to obtain and is presented as important for both fundamental understanding and engineering efforts.
the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.
High-resolution structural information on phototropins remains challenging to obtain and is presented as important for both fundamental understanding and engineering efforts.
the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.
Activation of the LOV2 domain triggers unfolding of alpha helices that communicate the light signal to the kinase domain.
activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain
Activation of the LOV2 domain triggers unfolding of alpha helices that communicate the light signal to the kinase domain.
activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain
Activation of the LOV2 domain triggers unfolding of alpha helices that communicate the light signal to the kinase domain.
activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain
Activation of the LOV2 domain triggers unfolding of alpha helices that communicate the light signal to the kinase domain.
activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain
Activation of the LOV2 domain triggers unfolding of alpha helices that communicate the light signal to the kinase domain.
activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain
Activation of the LOV2 domain triggers unfolding of alpha helices that communicate the light signal to the kinase domain.
activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain
Activation of the LOV2 domain triggers unfolding of alpha helices that communicate the light signal to the kinase domain.
activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain
Activation of the LOV2 domain triggers unfolding of alpha helices that communicate the light signal to the kinase domain.
activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain
Activation of the LOV2 domain triggers unfolding of alpha helices that communicate the light signal to the kinase domain.
activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain
Activation of the LOV2 domain triggers unfolding of alpha helices that communicate the light signal to the kinase domain.
activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Approval Evidence
2 sources2 linked approval claimsfirst-pass slug small-angle-x-ray-scattering
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis.
Source:
directly observed by small-angle X-ray scattering (SAXS)
Source:
structural modelsupports
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Source:
structural change observationsupports
Light-induced global conformational change of photoactive yellow protein was directly observed by small-angle X-ray scattering.
Source:
Comparisons
Source-backed strengths
The supplied evidence states that conformational changes were directly observed by SAXS. It is also presented as part of recent progress in studying multidomain phototropins from Chlamydomonas and Arabidopsis.
Compared with Avena sativa phototropin LOV2 domain
small-angle X-ray scattering and Avena sativa phototropin LOV2 domain address a similar problem space because they share signaling.
Shared frame: shared target processes: signaling; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Compared with caging/uncaging events
small-angle X-ray scattering and caging/uncaging events address a similar problem space because they share signaling.
Shared frame: shared target processes: signaling; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Strengths here: looks easier to implement in practice.
Compared with engineered focal adhesion kinase two-input gate
small-angle X-ray scattering and engineered focal adhesion kinase two-input gate address a similar problem space because they share signaling.
Shared frame: shared target processes: signaling; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Strengths here: looks easier to implement in practice.
Ranked Citations
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