Source 1primary paper2020UNC Libraries
Toolkit/isothermal titration calorimetry
isothermal titration calorimetry
Also known as: Isothermal titration calorimetry, ITC
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Isothermal titration calorimetry (ITC) is a thermal biophysical assay that quantifies binding-associated heat changes under isothermal conditions. In the cited study, ITC was used to support thermodynamic analysis of binding between CIB1 and α-integrin cytoplasmic tails.
Usefulness & Problems
Why this is useful
ITC is useful for experimentally characterizing biomolecular interactions through direct calorimetric readout of heat released or absorbed during binding. In the cited work, it provided thermodynamic support for analysis of CIB1 interactions with α-integrin cytoplasmic tails.
Problem solved
This assay helps address the problem of determining whether CIB1 binds α-integrin cytoplasmic tails and characterizing the thermodynamic basis of those interactions. The supplied evidence links ITC measurements to conclusions about hydrophobic interaction-driven binding and dependence on residues in the CIB1 consensus binding site.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
calorimetric detection of binding-associated heat changescalorimetric detection of binding-associated heat changesTarget processes
No target processes tagged yet.
Input: Thermal
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenoperating role: sensorswitch architecture: multi component
The assay operates under isothermal conditions and uses calorimetric detection of binding-associated heat changes. The provided evidence does not specify instrument model, sample concentrations, buffer conditions, protein preparation, or analysis workflow.
The supplied evidence is limited to a single study context involving CIB1 and α-integrin cytoplasmic tails. No implementation parameters, performance metrics, sensitivity limits, throughput characteristics, or independent replication are provided in the evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2025MED
Ranked Claims
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Approval Evidence
2 sources1 linked approval claimfirst-pass slugs isothermal-titration-calorimetry, isothermal-titration-calorimetry-for-teniposide-sting-binding
Direct binding of Teniposide to STING's cytosolic domain was confirmed via isothermal titration calorimetry (ITC).
Source:
Isothermal titration calorimetry measurements indicated
Source:
binding mechanismsupports
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Source:
Comparisons
Source-backed strengths
ITC provides a direct thermal measurement of binding-associated heat changes without requiring an optical reporter in the supplied description. In the cited study, ITC measurements supported mechanistic interpretation of CIB1 promiscuity toward multiple α-integrin cytoplasmic tails.
Compared with Field-domain rapid-scan EPR at 240 GHz
isothermal titration calorimetry and Field-domain rapid-scan EPR at 240 GHz address a similar problem space.
Shared frame: same top-level item type
Compared with fluorescence line narrowing
isothermal titration calorimetry and fluorescence line narrowing address a similar problem space.
Shared frame: same top-level item type
Compared with native green gel system
isothermal titration calorimetry and native green gel system address a similar problem space.
Shared frame: same top-level item type
Strengths here: looks easier to implement in practice.
Ranked Citations
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