The 4 Levels of a Protein (Basic info outline)

1. FOUR LEVELS OF STRUCTURE TO A PROTEIN
1. Primary

1.      sequence of amino acids

2.      held together by peptide bonds

3.      controls the shape it will fold into

2. Secondary

1.      repeated folding or coiling

2.      held together by hydrogen bonding

3.      Examples: alpha helices and beta pleated sheets

3. Tertiary

1.      Overall peptide shape after folding and coiling

2.      hydrogen bongs

3.      3. Disulfide bonds

4.       Van der Walls interactions

4. Quaternary

1.      Two or more combined peptides

2.      Final functional form

3.      Hydrogen bonding, disulfide bonds, Van de Waal interactions

    2.EACH LEVEL AFFECTS THE NEXT LEVEL OF STRUCTURE TO CREATE A SHAPE

A.     that fits together with other molecules that the protein catalyzes

B.     that carries out other functions such as structural roles

C.     One example of a functional protein is 

“Another example of a functional protein is a protein in egg whites called avidin. This functional protein binds biotin with great specificity and tenacity. Animals fed diets containing large amounts of egg white may become deficient in biotin, even though biotin is added to their diet. Heating (cooking) disrupts the three-dimensional structure of avidin so that it can no longer bind biotin. It’s a good reason not to eat raw eggs!” (1)

DEFINITIONS:

A functional protein: A. has the ability to carry out metabolic processes. B. Proteins that have biological activity can be referred to as “functional proteins.”

amino acid: An organic molecule possessing both carboxyl and amino groups. Amino acids serve as the monomers of polypeptides.

LINKS used:

1.

http://www.ag-nutrient.com/index.php?option=com_content&view=article&id=4019:what-is-a-functional-protein&catid=50:calf-and-heifer-raising&Itemid=76