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Which non-covalent forces are important in maintaining the tertiaty structure of these proteins? What experimental evidence...

Which non-covalent forces are important in maintaining the tertiaty structure of these proteins? What experimental evidence may this be based?

Which non-covalent forces are being effected in urea unfolding of protein?

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The most important non-covalent forces maintaining the tertiary structure of proteins is the hydrophobic effect. The hydrophobic/non-polar amino acids like to be buried within the globular core of the protein while the hydrophilic or polar side chains interact with the water (which is also polar). This is based on theory, not on experimental evidence. Urea decreases the hydrophobic effect and binds directly to amide units by forming hydrogen bonds.(Reference : Zou Q, Habermann-Rottinghaus SM, Murphy KP. Urea effects on protein stability: hydrogen bonding and the hydrophobic effect. Proteins. 1998 May 1;31(2):107-15)

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