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Updated: Mar 15, 2026
11:44
Spin Saturation Transfer Difference NMR SSTD NMR: A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes
Published on: November 12, 2016
18.7K
To Swap or Not To Swap
Gourisankar Ghosh1, Tapan Biswas1
1Department of Chemistry & Biochemistry, University of California-San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.
Structure (London, England : 1993)
|September 8, 2016
Summary
Domain swapping, a protein oligomerization process, was studied in hCREBPII. Researchers identified a key hydrogen bond and protein concentration as critical factors influencing protein form.
Area of Science:
- Biochemistry
- Structural Biology
- Protein Science
Background:
- Protein oligomerization involves the assembly of multiple protein subunits.
- Domain swapping is a specific oligomerization mechanism where structural units are exchanged between protein protomers.
Purpose of the Study:
- To investigate the formation of domain-swapped dimers of human CREB-binding protein II (hCREBPII).
- To identify critical factors regulating the balance between monomeric and dimeric forms of hCREBPII.
Main Methods:
- Analysis of protein structure and oligomerization states.
- Investigation of the role of specific molecular interactions, such as hydrogen bonds.
- Examination of the impact of protein concentration on oligomer formation.
Main Results:
- Domain-swapped dimers of hCREBPII were identified and characterized.
- A single hydrogen bond was pinpointed as crucial for the observed domain swapping.
- Protein concentration was found to be a significant regulator of the monomer/dimer equilibrium.
Conclusions:
- Domain swapping in hCREBPII is influenced by specific structural features and solution conditions.
- Understanding these regulators is key to comprehending protein assembly and function.
- This study provides insights into the molecular mechanisms governing protein oligomerization.
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