Abstract
The surface net hydrophobicity and local hydrophobicity of green fluorescent protein was evaluated by using the aqueous two-phase partitioning method. The surface net hydrophobicity of GFP allowed it to be classified as a hydrophobic protein although the local hydrophobicity was low. The local hydrophobicity of the GFP was increased by a pH shift to acidic conditions and was maximal at pH 4. The surface net hydrophobicity increased at acidic conditions less than pH 4. The conformational change of GFP at acidic pH is discussed based on the above results.
| Original language | English |
|---|---|
| Pages (from-to) | 145-150 |
| Number of pages | 6 |
| Journal | Solvent Extraction Research and Development |
| Volume | 16 |
| Publication status | Published - 2009 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Chemistry(all)
- Chemical Engineering(all)
Cite this
Characterization of green fluorescent protein using aqueous two-phase systems. / Umakoshi, Hiroshi; Nishida, Masato; Suga, Keishi; Bui, Huong Thi; Shimanouchi, Toshinori; Kuboi, Ryoichi.
In: Solvent Extraction Research and Development, Vol. 16, 2009, p. 145-150.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of green fluorescent protein using aqueous two-phase systems
AU - Umakoshi, Hiroshi
AU - Nishida, Masato
AU - Suga, Keishi
AU - Bui, Huong Thi
AU - Shimanouchi, Toshinori
AU - Kuboi, Ryoichi
PY - 2009
Y1 - 2009
N2 - The surface net hydrophobicity and local hydrophobicity of green fluorescent protein was evaluated by using the aqueous two-phase partitioning method. The surface net hydrophobicity of GFP allowed it to be classified as a hydrophobic protein although the local hydrophobicity was low. The local hydrophobicity of the GFP was increased by a pH shift to acidic conditions and was maximal at pH 4. The surface net hydrophobicity increased at acidic conditions less than pH 4. The conformational change of GFP at acidic pH is discussed based on the above results.
AB - The surface net hydrophobicity and local hydrophobicity of green fluorescent protein was evaluated by using the aqueous two-phase partitioning method. The surface net hydrophobicity of GFP allowed it to be classified as a hydrophobic protein although the local hydrophobicity was low. The local hydrophobicity of the GFP was increased by a pH shift to acidic conditions and was maximal at pH 4. The surface net hydrophobicity increased at acidic conditions less than pH 4. The conformational change of GFP at acidic pH is discussed based on the above results.
UR - http://www.scopus.com/inward/record.url?scp=69549103419&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=69549103419&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:69549103419
VL - 16
SP - 145
EP - 150
JO - Solvent Extraction Research and Development
JF - Solvent Extraction Research and Development
SN - 1341-7215
ER -