PROTEIN FOLDING

PROTEIN FOLDING

1. Proteins roles

   • Be involved with protecting the body
   • Be part of a structure
   • Sereves as enzimes for important biological processes
   • Make up channels

2. Structural levels

   • Primary structure
     • This is the sequence of amino acids that make up a protein.
       • In protein synthesis, amino acids are added to form a polypeptide chain and proteins are made of 1 or more of these polypeptide chains.
       • Amino acids are the monomer (which means the building block) of a protein.
       • Genes, which are made of DNA, determine the order and number of these amino acids.
       • One amino acid can be changed sickle cell disease
   • Secondary Structure
     • The sequence of amino acids that we mentioned in primary structure, can fold in different ways
       • The most common ways are the alpha helix and the beta pleated sheet and which one of these folding the protein does depends on the amino acid arrangement it has.
       • Those hydrogen bonds can occur at specific areas of the protein’s amino acids.
         • Both of these shapes are due largely in part to hydrogen bonds.
   • Tertiary Structure
     • This looks more folding that occurs in the 3D shape of a functional protein.
       • And a lot of this is due to something we called the R groups, also called side chains
       • The amino group and the carboxyl group are generally standard parts of an amino acid, although the R group found in amino acids can vary among different amino acids.
       • proteins contain many amino acids which can contain different R groups and so different areas of the protein can therefore be impacted based on those R groups.
   • Quaternary Structure
     • Proteins can be made of 1 or more polypeptide chains in quaternary structure
     • Each of these polypeptide chains can be a subunit and interactions between them such 05:19 as hydrogen bonds or disulfide bonds can keep them together.
     • The interactions mentioned like hydrogen bonds and R group interactions are occurring depending on the protein’s own amino acids.

3. Proteins have help in folding

   • Chaperonins, for example, are proteins that can help with the folding process.
     • They have almost a barrel shape.
     • Proteins go into them, and the chaperonin tends to have an environment that is ideal for the proteins’ folding.
     • This can help the protein to be folded correctly so it’s functional.
     • There are many diseases that are related to protein misfoldings.

4. Denaturing proteins

   • each protein has an ideal environment for functioning which might include a certain temperature or pH range.
   • If the protein is exposed to something outside of its ideal temperature or pH range- exposed to high heat for example- you can disrupt the interactions that we have talked about taking place at the different structural levels.
   • This can denature the protein, which disrupts its shape.
   • Depending on what caused it to be denatured, sometimes you are interfering with many levels of protein structure
   • The environment that a protein is in definitely matters for its functioning.

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