BIOC 2580 Lecture Notes - Lecture 6: Trypsin, Aldehyde, Collision Frequency
30 May 2016
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Document Summary
The normal folded state of a protein is called its native state essential for proper function. When unfolded a protein is said to be denatured loses all function. Covalent bonding links amino acids in a chain in a specific sequence. Non-covalent interactions dictate folding pattern and stability: hydrophobic effect and van der waals effect are the most important non-covalent interactions. Hydrophobic effect locates non polar amino acids in core of folded protein, aoiding unfavourable interaction with water: contributes ~50% of total energy stabilizing native state, -5kj. mol per ch, ch2, ch3 moved out of contact with water. Polar amino acids can face exterior, where interact well with water. Van der waals interaction is a weak electrostatic attraction between atoms that are close, but not covalently bonded to each other aka london dispersion forces. Random fluctuations in distribution of nucleus and electrons create short-lived dipoles, which induce dipole in close neighbours.
