Source 1review1987Journal of Bioenergetics and Biomembranes
Toolkit/deuterium NMR
deuterium NMR
Also known as: 2H NMR, deuterium magnetic resonance
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
protons in lipids and proteins have been selectively replaced by deuterons and the resultant deuterium NMR spectrum analyzed to give structural and dynamic information about the molecular associations between a range of membrane components
Usefulness & Problems
Why this is useful
Deuterium NMR analyzes spectra from deuteron-labeled membrane components to infer structural and dynamic features of molecular associations at membrane surfaces. The review frames it as a way to study organization at the polar-apolar interface of biomembranes.; characterizing lipid-protein interactions at membrane surfaces; probing membrane-surface organization architecturally and dynamically; studying molecular associations among lipids, proteins, and oligosaccharides
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Deuterium NMR analyzes spectra from deuteron-labeled membrane components to infer structural and dynamic features of molecular associations at membrane surfaces. The review frames it as a way to study organization at the polar-apolar interface of biomembranes.
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characterizing lipid-protein interactions at membrane surfaces
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probing membrane-surface organization architecturally and dynamically
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studying molecular associations among lipids, proteins, and oligosaccharides
Problem solved
It addresses the difficulty of studying specific interactions at membrane surfaces, where classical structural methods are said to be inappropriate for most membrane problems. It is used to obtain interfacial information linked to biochemical integrity and function.; provides structural and dynamic information about membrane interfacial associations in systems where classical structural methods are described as inappropriate
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It addresses the difficulty of studying specific interactions at membrane surfaces, where classical structural methods are said to be inappropriate for most membrane problems. It is used to obtain interfacial information linked to biochemical integrity and function.
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provides structural and dynamic information about membrane interfacial associations in systems where classical structural methods are described as inappropriate
Problem links
provides structural and dynamic information about membrane interfacial associations in systems where classical structural methods are described as inappropriate
LiteratureIt addresses the difficulty of studying specific interactions at membrane surfaces, where classical structural methods are said to be inappropriate for most membrane problems. It is used to obtain interfacial information linked to biochemical integrity and function.
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It addresses the difficulty of studying specific interactions at membrane surfaces, where classical structural methods are said to be inappropriate for most membrane problems. It is used to obtain interfacial information linked to biochemical integrity and function.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Target processes
No target processes tagged yet.
Input: Chemical
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: sensor
The method requires selective replacement of protons with deuterons in lipids or proteins and access to deuterium NMR spectral analysis. The abstract also implies membrane model systems were commonly used.; requires deuterated membrane components; requires analysis of deuterium NMR spectra; application to complex membrane surfaces is complicated by chemical heterogeneity
The abstract does not support that it broadly solves all membrane structural problems, and it notes most studies were limited to model systems. It also does not remove the risk that probing the surface perturbs the interactions being studied.; requires selective replacement of protons by deuterons; the majority of reported studies had been on model systems; membrane-surface probing is challenging because perturbation of the interactions under study can occur
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
In principle, deuterium NMR-based study can be applied to lipids, proteins, and oligosaccharides, with information related to biochemical integrity and function.
In principle, lipids, proteins, and oligosaccharides can be studied by this method and the information gained related to biochemical integrity and function.
The review states that X-ray diffraction, electron microscopy, and high-resolution 2D NMR techniques are inappropriate for all but the simplest membrane problems.
Classical methods for obtaining structural information about biomolecules, including X-ray diffraction, electron microscopy, and more recently high-resolution 2D nuclear magnetic resonance techniques are inappropriate for all but the simplest of membrane problems.
The review states that most studies reported so far were performed on model systems, with only one or two notable exceptions.
With one or two notable exceptions, the majority of the studies reported so far have been on model systems.
Deuterium NMR can provide structural and dynamic information about molecular associations among membrane components at biomembrane surfaces.
the resultant deuterium NMR spectrum analyzed to give structural and dynamic information about the molecular associations between a range of membrane components
The review highlights protein-lipid molecular specificity in membranes, peptide-induced lateral separation, and ionization behavior of deuterated phospholipids and peripheral proteins as topics demonstrated predominantly using deuterium NMR methods.
protein-lipid molecular specificity in membranes, peptide-induced lateral separation, and the ionization behavior of deuterated phospholipids and peripheral proteins will all be demonstrated predominantly using deuterium NMR methods
Approval Evidence
1 source5 linked approval claimsfirst-pass slug deuterium-nmr
protons in lipids and proteins have been selectively replaced by deuterons and the resultant deuterium NMR spectrum analyzed to give structural and dynamic information about the molecular associations between a range of membrane components
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applicabilitysupports
In principle, deuterium NMR-based study can be applied to lipids, proteins, and oligosaccharides, with information related to biochemical integrity and function.
In principle, lipids, proteins, and oligosaccharides can be studied by this method and the information gained related to biochemical integrity and function.
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comparative method positioningsupports
The review states that X-ray diffraction, electron microscopy, and high-resolution 2D NMR techniques are inappropriate for all but the simplest membrane problems.
Classical methods for obtaining structural information about biomolecules, including X-ray diffraction, electron microscopy, and more recently high-resolution 2D nuclear magnetic resonance techniques are inappropriate for all but the simplest of membrane problems.
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evidence boundarysupports
The review states that most studies reported so far were performed on model systems, with only one or two notable exceptions.
With one or two notable exceptions, the majority of the studies reported so far have been on model systems.
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method scopesupports
Deuterium NMR can provide structural and dynamic information about molecular associations among membrane components at biomembrane surfaces.
the resultant deuterium NMR spectrum analyzed to give structural and dynamic information about the molecular associations between a range of membrane components
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use case examplessupports
The review highlights protein-lipid molecular specificity in membranes, peptide-induced lateral separation, and ionization behavior of deuterated phospholipids and peripheral proteins as topics demonstrated predominantly using deuterium NMR methods.
protein-lipid molecular specificity in membranes, peptide-induced lateral separation, and the ionization behavior of deuterated phospholipids and peripheral proteins will all be demonstrated predominantly using deuterium NMR methods
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Comparisons
Source-stated alternatives
The abstract contrasts this approach with X-ray diffraction, electron microscopy, and high-resolution 2D NMR techniques, describing those as inappropriate for all but the simplest membrane problems.
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The abstract contrasts this approach with X-ray diffraction, electron microscopy, and high-resolution 2D NMR techniques, describing those as inappropriate for all but the simplest membrane problems.
Source-backed strengths
can report on both structural and dynamic information; can in principle be applied to lipids, proteins, and oligosaccharides; is presented as useful for relating interfacial organization to biochemical integrity and function
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can report on both structural and dynamic information
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can in principle be applied to lipids, proteins, and oligosaccharides
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is presented as useful for relating interfacial organization to biochemical integrity and function
Compared with electron microscopy
The abstract contrasts this approach with X-ray diffraction, electron microscopy, and high-resolution 2D NMR techniques, describing those as inappropriate for all but the simplest membrane problems.
Shared frame: source-stated alternative in extracted literature
Strengths here: can report on both structural and dynamic information; can in principle be applied to lipids, proteins, and oligosaccharides; is presented as useful for relating interfacial organization to biochemical integrity and function.
Relative tradeoffs: requires selective replacement of protons by deuterons; the majority of reported studies had been on model systems; membrane-surface probing is challenging because perturbation of the interactions under study can occur.
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The abstract contrasts this approach with X-ray diffraction, electron microscopy, and high-resolution 2D NMR techniques, describing those as inappropriate for all but the simplest membrane problems.
Compared with microscopy
The abstract contrasts this approach with X-ray diffraction, electron microscopy, and high-resolution 2D NMR techniques, describing those as inappropriate for all but the simplest membrane problems.
Shared frame: source-stated alternative in extracted literature
Strengths here: can report on both structural and dynamic information; can in principle be applied to lipids, proteins, and oligosaccharides; is presented as useful for relating interfacial organization to biochemical integrity and function.
Relative tradeoffs: requires selective replacement of protons by deuterons; the majority of reported studies had been on model systems; membrane-surface probing is challenging because perturbation of the interactions under study can occur.
Source:
The abstract contrasts this approach with X-ray diffraction, electron microscopy, and high-resolution 2D NMR techniques, describing those as inappropriate for all but the simplest membrane problems.
Ranked Citations
- 1.