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Effect of hydrophobicity score on stabilization by Macromolecular Crowding
Author(s) -
Kraft Shan,
Shell Elizabeth
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a637-b
Subject(s) - peg ratio , chemistry , myoglobin , bovine serum albumin , polyethylene glycol , macromolecule , macromolecular crowding , chromatography , biophysics , biochemistry , biology , finance , economics
The effects of the interaction between macromolecular crowding and hydrophobicity on the stability of various proteins under denaturing conditions were tested. Five different proteins, invertase, bovine albumin, hemoglobin, cytochrome C, and alpha‐1‐acid‐glycoprotein, with varying Grand Average of Hydropathicity (GRAVY) scores were used. The protein was added to different concentrations of polyethylene glycol (PEG), and the protein/PEG mixture was heated from 22 C to 80 C. The progress of the protein unfolding was monitored using UV‐Visible spectroscopy and fluorescence. It was found that the GRAVY score of the protein influenced the effect of PEG on the protein's stability. As the GRAVY score became more negative, which meant that the protein was more hydrophilic, the protein became more stable as the concentration of PEG increased. Inversely, proteins with more positive GRAVY scores were more unstable as the concentration of PEG increased.