Amino Acids Proteins, and Enzymes Types of Proteins Amino Acids The Peptide Bond Amino Acids Proteins, and Enzymes

Types of Proteins Type Examples Structural tendons, cartilage, hair, nails Contractile muscles Transport hemoglobin Storage milk Hormonal insulin, growth hormone Enzyme catalyzes reactions in cells Protection immune response

Amino Acids Building blocks of proteins Carboxylic acid group Amino group Side group R gives unique characteristics R side chain I H2H—C —COOH H

Examples of Amino Acids H I H2N—C —COOH H glycine CH3 H alanine

Types of Amino Acids Nonpolar R = H, CH3, alkyl groups, aromatic O Polar ll R = –CH2OH, –CH2SH, –CH2C–NH2, (polar groups with –O-, -SH, - N-) Polar/Acidic R = –CH2COOH, or -COOH Polar/ Basic R = –CH2CH2NH2

Learning Check AA1 A. NH2–CH2–COOH (Glycine) CH3 | CH–OH Identify each as (1) polar or (2) nonpolar A. NH2–CH2–COOH (Glycine) CH3 | CH–OH B. NH2–CH–COOH (Serine)

Solution AA1 A.(2) NH2–CH2–COOH (Glycine) CH3 | CH–OH Identify each as (1) polar or (2) nonpolar A.(2) NH2–CH2–COOH (Glycine) CH3 | CH–OH B. (1) NH2–CH–COOH (Serine)

Essential Amino Acids 10 amino acids not synthesized by the body arg, his, ile, leu, lys, met, phe, thr, trp, val Must obtain from the diet All in dairy products 1 or more missing in grains and vegetables

Amino Acids as Acids and Bases Ionization of the –NH2 and the –COOH group Zwitterion has both a + and – charge Zwitterion is neutral overall + NH2–CH2–COOH H3N–CH2–COO– glycine Zwitterion of glycine

pH and ionization H+ OH– + + Positive ion zwitterion Negative ion + + H3N–CH2–COOH H3N–CH2–COO– H2N–CH2–COO– Positive ion zwitterion Negative ion Low pH neutral pH High pH

The Peptide Bond Amide bond formed by the –COOH of an amino acid and the –NH2 of the next amino acid O CH3 + | | + | NH3–CH2–COH + H3N–CH–COO– O CH3 + | | | NH3–CH2–C – N–CH–COO– | peptide bond H

Peptides Amino acids linked by amide (peptide) bonds Gly Lys Phe Arg Ser H2N-end COOH-end Peptide bonds

Learning Check AA3 What are the possible tripeptides formed from one each of leucine, glycine, and alanine?

Solution AA3 Tripeptides possible from one each of leucine, glycine, and alanine Leu-Gly-Ala Leu-Ala-Gly Ala-Leu-Gly Ala-Gly-Leu Gly-Ala-Leu Gly-Leu-Ala

Amino Acids, Proteins, and Enzymes Primary and Secondary Structure Tertiary and Quaternary Structure Protein Hydrolysis and Denaturation

Primary Structure of Proteins The particular sequence of amino acids that is the backbone of a peptide chain or protein Ala-Leu-Cys-Met

Secondary Structure – Alpha Helix Three-dimensional arrangement of amino acids with the polypeptide chain in a corkscrew shape Held by H bonds between the H of –N- H group and the –O of C=O of the fourth amino acid along the chain Looks like a coiled “telephone cord”

Secondary Structure – Beta Pleated Sheet Polypeptide chains are arranged side by side Hydrogen bonds form between chains R groups of extend above and below the sheet Typical of fibrous proteins such as silk

Secondary Structure – Triple Helix Three polypeptide chains woven together Glycine, proline, hydroxy proline and hydroxylysine H bonding between –OH groups gives a strong structure Typical of collagen, connective tissue, skin, tendons, and cartilage

Learning Check P1 Indicate the type of structure as primary (2) alpha helix beta pleated sheet (4) triple helix Polypeptide chain held side by side by H bonds Sequence of amino acids in a polypeptide chain Corkscrew shape with H bonds between amino acids Three peptide chains woven like a rope

Solution P1 Indicate the type of structure as primary (2) alpha helix beta pleated sheet (4) triple helix 3 Polypeptide chain held side by side by H bonds 1 Sequence of amino acids in a polypeptide chain 2 Corkscrew shape with H bonds between amino acids 4 Three peptide chains woven like a rope

Tertiary Structure Specific overall shape of a protein Cross links between R groups of amino acids in chain disulfide –S–S– + ionic –COO– H3N– H bonds C=O HO– hydrophobic –CH3 H3C–

Globular and Fibrous Proteins Globular proteins Fibrous proteins “spherical” shape long, thin fibers Insulin Hair Hemoglobin Wool Enzymes Skin Antibodies Nails

Quaternary Structure Proteins with two or more chains Example is hemoglobin Carries oxygen in blood Four polypeptide chains Each chain has a haem group to bind oxygen

Learning Check P3 Identify the level of protein structure 1. Primary 2. Secondary Tertiary 4. Quaternary Beta pleated sheet Order of amino acids in a protein A protein with two or more peptide chains The shape of a globular protein Disulfide bonds between R groups

Solution P3 Identify the level of protein structure 1. Primary 2. Secondary 3. Tertiary 4. Quaternary 2 Beta pleated sheet 1 Order of amino acids in a protein 4 A protein with two or more peptide chains D. 3 The shape of a globular protein E. 3 Disulfide bonds between R groups

Protein Hydrolysis Break down of peptide bonds Requires acid or base and heat Gives smaller peptides and amino acids Similar to digestion of proteins using enzymes Occurs in cells to provide amino acids to synthesize other proteins and tissues

Hydrolysis of a Dipeptide

Denaturation Disruption of secondary, tertiary and quaternary protein structure by heat/organics Break apart H bonds and disrupt hydrophobic attractions acids/ bases Break H bonds between polar R groups and ionic bonds heavy metal ions React with S-S bonds to form solids agitation Stretches chains until bonds break

Applications of Denaturation Hard boiling an egg Wiping the skin with alcohol swab for injection Cooking food to destroy E. coli. Heat used to cauterize blood vessels Autoclave sterilizes instruments Milk is heated to make yoghurt

Learning Check P4 What are the products of the complete hydrolysis of Ala-Ser-Val?

Solution P4 The products of the complete hydrolysis of Ala-Ser-Val are alanine serine valine

Learning Check P5 Tannic acid is used to form a scab on a burn. An egg becomes hard boiled when placed in hot water. What is similar about these two events?

Solution P5 Acid and heat cause a denaturation of protein. They both break bonds in the secondary and tertiary structure of protein.

DNA

DNA RNA

DNA RNA

DNA RNA

DNA Backbone Structure Alternate phosphate and sugar (deoxyribose), phosphate ester bonds

DNA Backbone Structure Alternate phosphate and sugar (deoxyribose), phosphate ester bonds

DNA RNA

DNA Primary Structure Summary

DNA RNA

Base pairing by unique hydrogen bonds DNA Double Helix Base pairing by unique hydrogen bonds C - G and A - T pairs

Base pairing by unique hydrogen bonds DNA Double Helix Base pairing by unique hydrogen bonds C - G and A - T pairs

DNA

Complementary base pairs form new strands. DNA Replication Complementary base pairs form new strands.

Types of RNA mRNA contains codons which code for amino acids.

DNA

rRNA - Ribosome - contains enzymes and keeps everything together Types of RNA rRNA - Ribosome - contains enzymes and keeps everything together

Types of RNA tRNA - Transfer RNA carries amino acid and read codons on m-RNA through its own anticodons.

Types of RNA tRNA - Transfer RNA carries amino acid and read codons on m-RNA through its own anticodons.