Protein Structures There are 4 protein structures. Today you will be able to identify the proteins based on their structures and sequence of amino acids

Explanation of Protein Structures Check out this link for more detail.

Rules to remember... The sequence of the nucleotide determines the amino acid. The amino acid sequence determines the protein shape. The protein shape determines it function.

Primary Protein Structure Shaped like a chain.

Primary Primary protein structures refer to the order in which amino acids link together. Proteins combine to form a chain of amino acids. The amino acids include an alpha carbon, which is bonded to a Hydrogen atom, a carboxyl group and an amino group. Amino acid sequences of a protein are determined by the information found within the cellular genetic code. The order of amino acids within the polypeptide chain is completely unique, and is specifically linked to a protein. When amino acids are changed within a sequence, a gene mutation occurs, which often results in a protein that is non-functioning. Check out this link to learn more about primary protein structures.

Secondary Structure- refers to the coiling or folding of a polypeptide chain that gives the protein its 3-D shape.

Secondary Secondary protein structures occur when polypeptide chains coil or fold, giving them a 3D shape. Alpha(α)Helix structures resemble a coiled spring, and result from hydrogen bonding within the peptide chain. Beta Pleated structures seem to be folded, or pleated and form when hydrogen bonds between adjacent polypeptide units Check out this link to learn more about secondary protein structures.

Tertiary Protein Structure Hydrophobic interactions greatly contribute to the folding and shaping of a protein. The "R" group of the amino acid is either hydrophobic or hydrophilic. The amino acids with hydrophilic "R" groups will seek contact with their aqueous environment, while amino acids with hydrophobic "R" groups will seek to avoid water and position themselves towards the center of the protein.

Tertiary Tertiary protein structures deal with the 3D shape of a polypeptide chain. There are multiple bonds/forces that contribute to the protein’s ability to remain in tact. Hydrophobic interactions often play a key role in maintaining a protein’s shape. “R” groups in amino acids are either hydrophobic or hydrophilic and will seek aquatic or non-aquatic environments accordingly, which determines their location within the protein. Hydrogen bonds facilitate stabilization within the proteins based on the shape established by the hydrophobic interactions. Ionic bonding causes folding between positively and negatively charged R groups. Check out this link to learn more about tertiary protein structures.

Quaternary Structure Refers to the structure of a protein macromolecule formed by interactions between multiple polypeptide chains.

Quaternary Quaternary structures deal with the structures that between multiple polypeptide chains. Each chain is referred to as a subunit. Structures may consist of multiple polypeptide chains that may either be the same subunit, or different subunits. Click this link to learn more about quaternary protein structures.

Here are all of them together

Why do they change structures?

What can cause a protein structure to change? Changes in pH Changes in salt concentration Changes in temperature Presence of reducing agents

Where do you find these structures?

How has environmental changes impacted our need for different types of proteins? Small fire activity