| Region 1 |
| Type: | Disordered |
| Name: | mature COR15A |
| Location: | 51 - 139 |
| Length: | 89 |
| Region sequence: |
AKGDGNILDDLNEATKKASDFVTDKTKEALADGEKAKDYVVEKNSETADTLGKEAEKAAA
YVEEKGKEAANKAAEFAEGKAGEAKDATK |
| Modification type: | Native
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| PDB: | |
| Structural/functional type: | Function arises via a disorder to order transition
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| Functional classes: | |
| Functional subclasses: | Protein-lipid interaction
Protein-protein binding
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Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (or dried rCor15a 2 mg/mL; rCor15a (in H2O) 0.75 mg/mL)
- SDS-PAGE gel, Aberrant mobility on
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References:
- Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. "Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state." Biochim. Biophys. Acta. 2010; 1798(9): 1812-20. PubMed: 20510170
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Comments:Thalhammer et al (2010) found that both COR15A and COR15B are fully unstructured in solution, but gain alpha-helical structure upon drying.
To locate helices, the authors ran predictions which found alpha-helices predicted at about 58-81 and 97-137. Both helices appear to have amphipathic nature.
Experiments were performed on mature COR15A and mature COR15B without the signal peptides.
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