๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Contribution of the hydrophobic effect to globular protein stability

โœ Scribed by C.Nick Pace


Book ID
115985659
Publisher
Elsevier Science
Year
1992
Tongue
English
Weight
754 KB
Volume
226
Category
Article
ISSN
0022-2836

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Contribution of protein hydrophobicity t
โœ Nakai, S. ;Li-Chan, E. ;Hayakawa, S. ๐Ÿ“‚ Article ๐Ÿ“… 1986 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 534 KB

HANSCH analysis for quantitative structure-activity relationship (QSAR) was applied to aspartyl proteinases and it was found that higher hydrophobicity, tighter molecular structure, and lower charge are required for milk clotting enzymes compared to proteolytic enzymes. For simplicity in analysis of

Estimation of the stability of globular
โœ Faizan Ahmad; Charles C. Bigelow ๐Ÿ“‚ Article ๐Ÿ“… 1986 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 552 KB

The interpretation of A C 3 O (the free energy change for the reaction, globular conformation + randomly coiled conformation, in the absence of denaturant), in terms of the free energies of transfer of various parts of the protein molecule from water to denaturant solution, is unsatisfactory because