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The page below is a sample from the LabCE course Precision Medicine-Molecular Mechanisms of Cancer Development and Actionable Genes. Access the complete course and earn ASCLS P.A.C.E.-approved continuing education credits by subscribing online.

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The shape of a protein is extremely important as the specific shape is needed to perform a specific task. The shape of a protein dictates the job that can be done by that protein. Loss or change of shape will hinder the ability of the protein to do the job that it was created for. Proteins form a specific shape by folding in a way that allows bonds to form between specific amino acids.
Amino acids bound together by peptide bonds to make up a polypeptide are considered the primary structure of the protein. The secondary structure is created by hydrogen bonding across the amino acid chain to create two types of structures: alpha-helices and beta-sheets. The tertiary structure is driven by interactions between amino acids in the protein sequence and their affinity for water. Some amino acids are hydrophilic, meaning they are attracted to water and others are hydrophobic, meaning they repel water. The protein will fold such that amino acids that repel water are internal to the structure and proteins with an affinity for water are on the protein surface. Remember protein formation is occurring in the cytoplasm of the cell which is mainly composed of water. The tertiary structure ultimately determines the 3-dimensional shape of the protein. Quaternary structure is created when multiple polypeptides interact to form a complex for a single purpose. This occurs frequently in the cell; one example of a protein with quaternary structure is a receptor on the cell surface with two identical subunits.