| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7561355 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2011 | 10 Pages |
Abstract
⺠Thermal denaturation behavior of GFP is remarkably different from that of BCA-II. ⺠The inside of the GFP β-can is involved in intensive interactions with water molecules. ⺠At high temperatures, the GFP structure does not unfold but breaks. ⺠Irreversible thermal denaturation GFP is accompanied by massive aggregation. ⺠No accumulation of soluble denatured protein is detected.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Bogan S. Melnik, Nikolay V. Molochkov, Dmitry A. Prokhorov, Vladimir N. Uversky, Viktor P. Kutyshenko,