MBB 222 Study Guide - Final Guide: Guanidinium Chloride, Pancreatic Ribonuclease, Alpha Helix

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Denatured proteins have a loss of 3-d structure sufficient to cause loss of function. Denatured proteins exist in a partially folded state under most conditions. An unfolded protein is a protein that is completely unfolded. U9-07 must thermal denaturation; denaturing agents: urea, guanidine hydrochloride. Most proteins can be denatured by heat. Proteins can also denatured by ph extremes certain solutes (denaturing agents) such as urea and guanidine hydrochloride. These work by primarily disrupting the hydrophobic interactions that make up the stable core of globular proteins. Urea also disrupts the hydrogen bonds as the extremes of ph alter the net charge of the protein causing electrostatic repulsion and disruption of some h-bonding. Proteins will clump (aggregate) together when they are denatured, as the hydrophobic surfaces associate. The process of certain globular proteins returning to their native structure after being denatured. This occurs when the biological activity is returned to conditions where the native conformation is stable.