Source 1primary paper2012Journal of the American Chemical Society
Toolkit/reverse cross-saturation NMR methodology
reverse cross-saturation NMR methodology
Also known as: cross-saturation NMR experiments, reverse methodology
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Reverse cross-saturation NMR methodology is an NMR assay approach that maps the binding interface on a larger binding partner by applying selective radio-frequency irradiation to a smaller binding partner. In the cited study, irradiation of the αIIb peptide enabled detection of the interaction surface on Ca2+-bound CIB1.
Usefulness & Problems
Why this is useful
This methodology is useful for defining protein-peptide interaction surfaces when the larger partner is the interface-mapped species. The source study further states that it has broad potential for complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
Source:
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
Problem solved
It addresses the problem of identifying the binding interface on a larger protein within a heteromeric complex by reversing the usual cross-saturation irradiation scheme and irradiating the smaller partner instead. The demonstrated case involved the αIIb peptide and Ca2+-CIB1.
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.
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenoperating role: sensorswitch architecture: multi componentswitch architecture: recruitment
The demonstrated implementation used selective radio-frequency irradiation of the smaller binding partner, specifically the αIIb peptide, in an NMR cross-saturation experiment. The source indicates applicability to complexes containing synthetic peptides and suitably isotope-labeled medium- to large-sized proteins; no additional construct, buffer, or instrument parameters are provided here.
The supplied evidence is limited to a single reported application in the αIIb peptide-Ca2+-CIB1 complex and a general statement of potential broader use. No comparative performance metrics, sensitivity limits, or independent replication are provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
Approval Evidence
1 source2 linked approval claimsfirst-pass slug reverse-cross-saturation-nmr-methodology
in the NMR cross-saturation experiments, we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
Source:
method capabilitysupports
A reverse cross-saturation NMR methodology can detect the binding interface on a larger binding partner by selectively irradiating the smaller binding partner.
we applied the selective radio frequency irradiation to the smaller binding partner (the αIIb peptide), and successfully detected the binding interface on the larger binding partner Ca(2+)-CIB1
Source:
method generalizabilitysupports
The reverse cross-saturation methodology has broad potential for studying other complexes involving synthetic peptides and suitably isotope-labeled medium- to large-sized proteins.
This 'reverse' methodology has a broad potential to be employed to many other complexes where synthetic peptides and a suitably isotope-labeled medium- to large-sized protein are used to study protein-protein interactions.
Source:
Comparisons
Source-backed strengths
The method was reported to successfully detect the binding interface on the larger partner, Ca2+-CIB1, upon selective irradiation of the smaller αIIb peptide. The source also claims broader applicability to other complexes containing synthetic peptides and isotope-labeled medium- to large-sized proteins.
Compared with electron-transfer/higher-energy collision dissociation
reverse cross-saturation NMR methodology and electron-transfer/higher-energy collision dissociation address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization
Strengths here: looks easier to implement in practice.
Compared with higher-energy collisional dissociation
reverse cross-saturation NMR methodology and higher-energy collisional dissociation address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization
Compared with top-down mass spectrometry
reverse cross-saturation NMR methodology and top-down mass spectrometry address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization
Strengths here: looks easier to implement in practice.
Ranked Citations
- 1.