Protein

1. Protein

2. Amino Acids: Monomers of Proteins • A protein is a macromolecule that is made of monomers called Amino acids • Amino acids have an Amino group, Carboxyl group, a Hydrogen atom, and a Carbon chain, all connected to a central Carbon atom.

3. Amino Acids: Monomers of Proteins • All amino acids have the same base structure so to distinguish them you have to look at the carbon chain attached. • The C=O, C-O, C-N, and N-H bonds are all polar, therefore all amino acids are somewhat polar.

4. Amino Acids: Monomers of Proteins • Some are more polar than others due to the polarity of the carbon chain that is attached.

5. Amino Acids: Monomers of Proteins • There are 20 common amino acids that make up most proteins.

6. Amino Acids: Monomers of Proteins • 8 of them are called “Essential amino acids”, because they can't be produced by our bodies and need to be taken in our everyday food.

7. Amino Acids: Monomers of Proteins • These are Leucine, Lysine, Methionine, Phenylalanine, Theronine, Tryptophan, and Valine • Amino acids are linked through covalent bonds called “Peptide bonds”.

8. Amino Acids: Monomers of Proteins • Peptide bonds are formed between the Amino group of one amino acid to the Carboxyl group of another amino acid. • A polymer of amino acids is called a “Polypeptide”. • Proteins are made of one or more polypeptides

9. Amino Acids: Monomers of Proteins • There are many possible combinations to amino acids. • Ex. if a chain of 50 amino acids come together to make a protein, the possible combinations are

10. Nucleic Acids • An important class of macromolecules is nucleic acids. • There are two types of nucleic acids: DNA (deoxyribonucleic acid) and RNA (ribonucleic acid).

11. Nucleic Acids • The DNA contains the genetic information of an organism. This information is decoded into particular amino acid sequences of proteins, which carry out the many functions in the cell. • The transfer of genetic information stored in the DNA to the amino acid sequence of proteins is done with the help of RNA molecules.

12. Nucleic Acids • Both DNA and RNA molecules are composed of thousands of repeating nucleotide monomers. • A nucleotide is composed of these three components covalently bonded together: • A phosphate group • A sugar with five carbon atoms • A nitrogen-containing base

13. Nucleic Acids • The difference between DNA and RNA is the fact that the nucleotides in DNA contain the sugar deoxyribose and the nucleotides in RNA contain ribose. • There are 4 types of nitrogenous bases in DNA: • (A) adenine • (T) thymine • (G) guanine • (C) cytosine

14. Nucleic Acids • The same goes for RNA except for thymine (T), is replaced by uracil (U).

15. Levels of Protein Organization

16. Levels of Protein Organization • There are 4 levels that a protein structure is divided into • Primary Structures • Secondary Structures • Tertiary Structures • Quaternary Structures

17. Levels of Protein Organization • Primary Structure • It’s the linear sequence of amino acids • Peptide bonds linking amino acids is also seen as the back bone of a POLYpeptide chain

18. Levels of Protein Organization • Peptide bonds are polar and hydrogen bonds are possible between the C = O of one amino acid and the N-H of another

19. Levels of Protein Organization • Secondary Structures • A polypeptide can form a (alpha) helix or a folded fan shape (beta) pleated sheet

20. Levels of Protein Organization • Tertiary Structures • Created by a complex process of folding protein structures • The folding occurs naturally as the peptide bonds and other groups react to each other in the peptide chain

21. Levels of Protein Organization • Hydrophobic effect: Hydrophilic groups are directed aqueous environments. Hydrophobic groups are directed to the interior of protein’s three dimensional shape.

22. Levels of Protein Organization • Scientist now know the process of protein folding because of a class of protein called molecular chaperones. • These proteins interact with polypeptide chains and reproduce the folding process.

23. Levels of Protein Organization • Proteins with multiple polypeptide chains are quaternary structures. • In some conditions proteins unfold • Denaturation occurs when the normal bonding between groups is disturbed. • Intermolecular bonds break, possibly affecting secondary, tertiary and quaternary structures

24. Levels of Protein Organization • Conditions that cause denaturation include extreme hot or cold temperatures or exposure to certain chemical • Once a protein loses it’s normal 3-D structure it can’t preform its usual functions.