Solvent and temperature effects on crambin, a hydrophobic protein
نویسندگان
چکیده
منابع مشابه
Solvent structure at a hydrophobic protein surface.
The impact of an extensive, uniform and hydrophobic protein surface on the behavior of the surrounding solvent is investigated. In particular, focus is placed on the possible enhancement of the structure of water at the interface, one model for the hydrophobic effect. Solvent residence times and radial distribution functions are analyzed around three types of atomic sites (methyl, polar, and po...
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متن کاملThe glassy state of crambin and the THz time scale protein-solvent fluctuations possibly related to protein function
BACKGROUND THz experiments have been used to characterize the picosecond time scale fluctuations taking place in the model, globular protein crambin. RESULTS Using both hydration and temperature as an experimental parameter, we have identified collective fluctuations (<= 200 cm(-1)) in the protein. Observation of the protein dynamics in the THz spectrum from both below and above the glass tra...
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The Lum-Chandler-Weeks theory of hydrophobicity [Lum, K., Chandler, D. & Weeks, J. D. (1999) J. Phys. Chem. 103, 4570-4577] is applied to treat the temperature dependence of hydrophobic solvation in water. The application illustrates how the temperature dependence for hydrophobic surfaces extending less than 1 nm differs significantly from that for surfaces extending more than 1 nm. The latter ...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1980
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(80)84924-1