Protein stabilization by hydrophobic interactions at the surface
نویسندگان
چکیده
منابع مشابه
Protein stabilization by hydrophobic interactions at the surface.
The contribution of the solvent-exposed residue 63 to thermal stability of the thermolysin-like neutral protease of Bacillus stearothermophilus was studied by analyzing the effect of twelve different amino acid substitutions at this position. The thermal stability of the enzyme was increased considerably by introducing Arg, Lys or bulky hydrophobic amino acids. In general, the effects of the mu...
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Our goal was to gain a better understanding of the contribution of hydrophobic interactions to protein stability. We measured the change in conformational stability, Δ(ΔG), for hydrophobic mutants of four proteins: villin headpiece subdomain (VHP) with 36 residues, a surface protein from Borrelia burgdorferi (VlsE) with 341 residues, and two proteins previously studied in our laboratory, ribonu...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1994
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1994.tb18702.x