Michelle's Organic Chapter 15

Front 1

Proteins are VERY LARGE molecules which are important for all the following functions

Back 1

growth, maintenance, and replacement of body tissue

Front 2

Functions of proteins

Enzymes are proteins that catalyze most biochemical reactions

Back 2

Enzyme catalysis

Front 3

Functions of proteins

Enzymes are proteins that catalyze most biochemical reactions

Back 3

Enzyme catalysis

Front 4

Functions of Proteins

Hemoglobin is a protein that transports oxygen in the body; Ferritin is a protein that transports (from the blood plasma to the liver) and stores (in the liver) iron in the body

Back 4

Transport and storage

Front 5

Functions of enzymes

Actin and Myosin are proteins that provide muscle expansion and contraction

Back 5

Coordinated motion

Front 6

Functions of Enzymes

Collagen, Keratin, and other proteins are the chief constituents of skin, bone, hair, and fingernails

Back 6

Structural

Front 7

Functions of Enzymes

Antibodies are proteins that protect the body from foreign substances called antigens and help the body fight diseases

Back 7

Immune protection

Front 8

Functions of enzymes

Insulin, Oxytocin, and other proteins are hormones

Back 8

Hormones

Front 9

Functions of Enzymes (last one!)

Receptor proteins mediate the response of nerve cells to specific stimuli

Back 9

Generation and transmission of nerve impulses

Front 10

_______ are the building blocks of proteins.

Back 10

Amino acids

Front 11

Amino acids are composed of a ___________ and a _______________.

Back 11

amine and a carboxylic acid

Front 12

How many COMMON amino acids are there?

Back 12

20

Front 13

If all amino acids have the amine and the carboxyllic acids, what makes 20 DIFFERENT amino acids?

Back 13

The group found on the "R" or side group

Front 14

How many ESSENTIAL amino acids are there?

Back 14

10

Front 15

Amino acids are classified according to the ‘R’ group

Back 15

Nonpolar ‘R’ group – These amino acids contain a nonpolar hydrocarbon chain and are hydrophobic (not souble in water)

Alcohol ‘R’ group – These amino acids contain an alcohol (-OH)

Thiol (Sulfur) ‘R’ group – These amino acids contain a sulfur

Basic ‘R’ group – These amino acids contain an amine

Acidic ‘R’ group – These amino acids contain a carboxylic acid

Aromatic ‘R’ group – These amino acids contain a benzene ring

Amide ‘R’ group – These amino acids contain an amide

Front 16

What do we know about the acidity/basicity of an amino acid?

Back 16

Amino acids can act as an acid (Carboxyllic acids) or a base (amine).

Front 17

Because the molecule has regions of acidity and basicity, amino acids are GOOD ___________

Back 17

BUFFERS

Front 18

Amino acids have ions that have both a negative and a positive charge within the same structure... these structures are called

Back 18

Zwitterions

Front 19

At what pH does a protein act as a zwitter ion (contain both + and - ions)

Back 19

AT ITS ISOELECTRIC POINT

(different pH for each amino acid)

Front 20

At pH’s lower than the isoelectric point, the amino acid is

Back 20

a positive ion

Front 21

At pH’s higher than the isoelectric point, the amino acid is

Back 21

a negative ion

Front 22

______ are molecules that contain two or more amino acids

Back 22

Peptides

Front 23

_____ are polypeptides with more than 50 amino acids joined together

Back 23

Proteins

Front 24

What are the FOUR levels of protein structure

Back 24

Primary
Secondary
Tertiary
Quatenary

Front 25

The primary structure of a protein is determined by

Back 25

the sequence of amino acids

-what amino acids come after eachother will dictate how the molecule will look.

Front 26

The secondary structure of proteins is

Back 26

more involved with the folding and the geometric space occupied by the amino acids

Front 27

What are two common SECONDARY PROTEIN STRUCTURES?

Back 27

Alpha helix
Beta pleaded sheets

Front 28

The tertiary structure of a protein is

Back 28

a proteins three dimensional structure

Front 29

Tertiary structure of a protein is mantained by

Back 29

R group or side chain interactions

Front 30

What are the four types of tertiary interactions in proteins

Back 30

Covalent Cross Linkages or Disulfide Linkages

Hydrogen Bonding

Salt bridges

Hydrophobic Interactions

Front 31

The quaternary structure of proteins is

Back 31

the way that proteins with more than one polypeptide chain fit together

Front 32

What is the denaturation of proteins?

Back 32

When a protein looses its biological abilities

Front 33

What are common causes of denaturation?

Back 33

Heat
pH
Salinity
Heavy metals
Organic solvents
Reducing agents

Front 34

What is the sequence in which proteins are hydrolyzed

Back 34

Proteins --> Peptides --> Amino acids

(breaking down proteins)