| Region 1 |
| Type: | Disordered - Molten Globule |
| Name: | |
| Location: | 1 - 99 |
| Length: | 99 |
| Region sequence: |
MIEKLAEIRKKIDEIDNKILKLIAERNSLAKDVAEIKNQLGIPINDPEREKYIYDRIRKL
CKEHNVDENIGIKIFQILIEHNKALQKQYLEETQNKNKK |
| Modification type: | Engineered
Monomeric
|
| PDB: | |
| Structural/functional type: | Function arises via a disorder to order transition
|
| Functional classes: | Modification site
|
| Functional subclasses: | Substrate/ligand binding
|
Detection methods:
- Nuclear magnetic resonance (NMR) (293 K; pH: 6.5; sodium chloride 50 mM; sodium phosphate 20 mM)
- Circular dichroism (CD) spectroscopy, near-UV (293 K; )
- Fluorescence polarization/anisotropy (293 K; ANS 2 uM)
- Hydrogen-deuterium exchange (298 K; D2O (pD 7.4); NaCl (pH 6.7) 40 mM; sodium phosphate 2.5 mM)
- Mass spectrometry-based high resolution hydrogen-deuterium exchange
|
References:
- MacBeath G, Kast P, Hilvert D. "Redesigning enzyme topology by directed evolution." Science. 1998; 279(5358): 1958-61. PubMed: 9506949
- Vamvaca K, Vogeli B, Kast P, Pervushin K, Hilvert D. "An enzymatic molten globule: efficient coupling of folding and catalysis." Proc Natl Acad Sci U S A. 2004; 101(35): 12860-4. PubMed: 15322276
|
Comments:In the Vamvaca et al. paper, the six terminal amino acid residues of the protein were replaced by the following sequence: LEHHHHHH.
|
