Albumin coagulated when heated, which is precipitated at the iso-electric point, when acetic acid is added.
pHToo much charge can cause high electrostatic repulsion between charged amino acids and the protein structure is broken up
A charge is very unfavorable in the hydrophobic protein interior
Alcohol denatures protein by disrupting the side chain intramolecular hydrogen bonding. New hydrogen bond is formed inside between the new alcohol molecule and the protein side chain.
Heavy metal salt will neutralize the protein. By the negative charge of protein will bind with positive charge of metal ion. Then the protein will precipitate as insoluble metal protein salt.