Molecular Mechanisms of The Anomalous Thermal Aggregation of Green Fluorescent Protein
Green Fluorescent Protein, Carbonic Anhydrase II, NMR, Spin Diffusion, Protein Association, Protein–solvent Interaction
Digital Object Identifier (DOI)
The peculiarities of thermal denaturation and interaction with water of the cycle-3 mutant of green fluorescent protein (GFP) were analyzed by NMR techniques and compared with those of bovine carbonic anhydrase II (BCA-II). Irreversible thermal denaturation was accompanied by massive GFP aggregation with no detectable accumulation of soluble denatured protein. Analysis of the spin diffusion data suggested that the internal part of the GFP β-can is involved in intensive interactions with water molecules. As a result, at high temperatures, the GFP structure does not unfold but rather breaks, consequently leading to enhanced protein aggregation. This is very different from typical BCA-II behavior.
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Citation / Publisher Attribution
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, v. 1814, issue 12, p. 1930-1939
Scholar Commons Citation
Melnik, Bogdan S.; Molochkov, Nikolai V.; Prokhorov, Dmitry A.; Uversky, Vladimir N.; and Kutyshenko, Victor P., "Molecular Mechanisms of The Anomalous Thermal Aggregation of Green Fluorescent Protein" (2011). Molecular Medicine Faculty Publications. 489.