OBJECTIVE The objective of this experiment is to determine the effect of ammonium sulfate concentration towards protein precipitation

INT O!"CTION #rotein precipitation can be occurred b$ h$drophobic a%%re%ation& This can be happened b$ disruptin% the folded structure of the protein and exposin% more of the h$drophobic interior to the solution and also can be happened b$ deh$dratin% the shells of water molecules that form over h$drophobic patches on the surface of properl$ folded proteins& Once the proteins start a%%re%atin% into lar%er structures' the amount of water per protein will be drops' enhancin% the densit$ differences between the proteins and the solute& Once these a%%re%ates %row lar%e enou%h' it will disrupt the path of li%ht throu%h the solution' %ivin% it a cloud$ appearance& In addition' the densit$ differences become %reat enou%h for the a%%re%ates to be readil$ pellet in the centrifu%e& Because these methods depend on the protein molecules (findin%) one another in solution and formin% these a%%re%ates' the efficienc$ of this method depends on the concentration of the protein bein% precipitated& *hen the concentration is low' more harder for it to form a%%re%ates& #ractical rea%ents that has been used in this experiment to precipitate proteins is ammonium sulfate& +altin% proteins out of solution was discovered over ,-. $ears a%o b$ /ran0 1ofmeister when he noticed that the addition of different salts caused precipitate to form in solutions of e%% whites& 1e ordered the anions and cations b$ their abilit$ to precipitate proteins in what is 2nown as the 1ofmeister series& The current' mostl$3accepted

mechanism sa$s that saltin% proteins out of solution occurs when the water molecules are titrated awa$ from the solvent shells around the protein to the solvent shells around the ions that ma2e up the salt& +alts hi%h in the 1ofmeister series are the most efficient at protein precipitation because of the lar%e' stable solvent shells the$ maintain& This increases the surface tension of the solution' which effectivel$ increases the h$drophobic effect' which also stabili0es the protein structure while at the same time encoura%in% the h$drophobic re%ions on the surfaces of different molecules to interact' effectin% a%%re%ation& Because of this' proteins with a lar%er amount of h$drophobic surface character precipitate at lower salt concentrations than one with little h$drophobic surface character' and these protein to protein differences are exploited durin% protein purification procedures&