Chapter 3

Front 1

Protein Monomers

Back 1

1. Contain C, H, O, N and usually S

2. Proteins consist of 1 or more polypeptides.

3. Building block, or monomer is called amino acid.

4. Has Carboxyl, amino group, and side chain, and R group.

Front 2

Use EN to determine polarity

Back 2

H = C = S < N < O

Front 3

Peptide

Back 3

1. A linear chain of covalently linked aa. More than 50 aa = polypeptide.

Front 4

Proteins

Back 4

1. polymer made of monomers of amino acids

Front 5

Protein Structure

Back 5

1. Hierarchical structure.
2. Link amino acids.

3. Dyhyrdation reaction forms a peptide bond and water.

Front 6

Groups for Proteins

Back 6

1. C = 0 is the carbonyl group.

2. N - H is the amino group

3. R group points in different directions

Front 7

Primary Structure

Back 7

1. Sequence of amino acids.

Front 8

Secondary Structure

Back 8

1. repeating folding patterns stabilized by H bonds between carbonyl group of 1 aa and the amide group of another nonadjacent aa .

2. R groups are not involved in the H bond formation but their shape and charge makes the 2 degree structure.

3. Alpha Helix: each carbonyl group H bonds with an amide group 4 amino acids ahead in polymer

4. Beta-pleated sheet: The polypeptide folds back on itself; H bonds form between carbonyl groups in 1 part of polymer and amide in another

Front 9

Tertiary Structure

Back 9

1. Polypeptide folds into a 3-D shape because of R group interactions

2. Could be final level of structure for a protein

Front 10

R Group interactions

Back 10

Covalent bonds, ionic bonds, H bonds, hydrophobic effects, Von der Waals forces.

Front 11

Quatenary Structure

Back 11

1. Some proteins have this type of structure.

2. 2 or more polypeptides associates to form a functional multimark protein.

3. Subunits may be identical or different.

Front 12

Protein structure and function

Back 12

1. Are diverse.

2. A proteins function is reflective in its structure.