Proteins

Question 1

What makes a protein?

Answer 1

Amino acid

Question 2

What amino group does protein have?

Answer 2

Nitrogen and hydrogen

Question 3

Type of acid group protein has?

Answer 3

Carboxylic acid

Question 4

Where does the substituent R belong?

Answer 4

Alpha carbon

Question 5

What is the only form active in biological systems?

Answer 5

L-amino acids

Question 6

What amino acid does not have a stereoisomer?

Answer 6

Glycine

Question 7

Why does glycine not have a stereoisomer?

Answer 7

The functional group on glycine is a hydrogen making it a CH2 (not a chiral).

Question 8

What happens in a Thiol?

Answer 8

Has a sulfur and hydrogen.

Question 9

What happens in a alcohol?

Answer 9

Oxygen and hydrogen

Question 10

What type of amino acid is Cystine?

Answer 10

Polar amino acid

Question 11

What type of amino acid is Glycine?

Answer 11

Non polar amino acid

Question 12

What describes cystine?

Answer 12

Sulfhydryl and thiol

Question 13

Nonpolar amino acids have what type of intermolecular forces?

Answer 13

Dispersion force

Question 14

What amino acid can act as a buffer?

Answer 14

Basic and acidic amino acids.

Question 15

What amino acids form ions?

Answer 15

Basic and Acidic amino acids.

Question 16

What is a zwitterion?

Answer 16

Ion carrying both a positive and negative charge .

Question 17

Reason for zwitterions?

Answer 17

Non ionized form doesn’t exist.

Question 18

What happens with Cysteine?

Answer 18

It can oxidize and produce disulfide linkage

Question 19

What is a disulfide linkage in Cysteine?

Answer 19

When 2 cysteine make a covalent bond.

Question 20

To make a polypeptide backbone/protein, what chemical property has to occur?

Answer 20

Condensation

Question 21

How many amino acid residues in insulin?

Answer 21

51

Question 22

What happens when the amino acid residues connect in insulin?

Answer 22

It is no longer an amino acid

Question 23

It is only an amino acid when it is ___?

Answer 23

Free floating

Question 24

What is the opposite of condensation?

Answer 24

Hydrolysis

Question 25

How to get amino acid back out?

Answer 25

Hydrolyze the protein.

Question 26

Hydrolysis occurs under acidic or basic conditions?

Answer 26

Acidic conditions

Question 27

What happens when we eat protein?

Answer 27

Stomach acid hydrolyzes it (breaks it down)

Question 28

How do you disrupt a primary structure?

Answer 28

Hydrolysis

Question 29

What structure are A-helix and B-sheet?

Answer 29

Secondary structures

Question 30

As a secondary structure,what are they governed by?

Answer 30

Hydrogen bonding

Question 31

What are primary structures?

Answer 31

List of amino acid residues

Question 32

What are tertiary structures?

Answer 32

Overall 3D shape

Question 33

What are quaternary structures?

Answer 33

Multiple subunits combining together to form a larger protein

Question 34

What is a peptide bond?

Answer 34

A bond that occurs when oxygen as polysaccharide or disaccharide has a glycocidic linkage.

Question 35

What is a peptide linkage?

Answer 35

An amide linkage only when talking abt peptides.

Question 36

What do amino acid residues specifically make?

Answer 36

Peptide linkages which are a type of amide.

Question 37

What can amide be made of?

Answer 37

Anything that has nitrogen or carboxylic acid. When talking about amino acids = peptide linkages (formed)

Question 38

What is the peptide linkage name purpose? What is the reaction?

Answer 38

What brings them together and reaction is condensation reaction (water is produced, requires heat/enzyme)

Question 39

Is insulin a protein or polypeptide?

Answer 39

Polypeptide

Question 40

How many amino acid residues in a polypeptide?

Answer 40

50

Question 41

What is a fibrous classification?

Answer 41

Muscles, hair, etc..

Question 42

What is a globular classification?

Answer 42

Insulin, hemoglobin, etc.. (globs around)

Question 43

What is the size of proteins?

Answer 43

6000 to 10^6 amu

Question 44

Are proteins too large or small to pass through cell membranes?

Answer 44

Too large

Question 45

What happens when you end up with a lot of proteins in your blood?

Answer 45

Something bad happened to that cell to let proteins in blood.

Question 46

What behaves as buffers in proteins!

Answer 46

Isoelectric points

Question 47

What happens when changing the pH in proteins?

Answer 47

It can denature them

Question 48

What are isoelectric points?

Answer 48

The point of which the net overall charge of 0

Question 49

Functions of proteins?

Answer 49

Catalytic, structural, and storage, protective, regulatory, nerve impulse transmission, movement, and transport

Question 50

Catalytic function

Answer 50

Proteins acting as enzymes facilitating biochemical reactions w/ increased rates and specificity

Question 51

Structural function

Answer 51

All structure in body is protein. (Ex:collagen and keratin)

Question 52

Storage function

Answer 52

Proteins can store ions and molecules (ex: ferritin =storage of iron, ovalbumin=storage of amino acids in birds)

Question 53

Protective function

Answer 53

Proteins protect body from antibodies to clotting factors

Question 54

Regulatory functions

Answer 54

Proteins and peptides regulate processes in the form of hormones.

Question 55

Nerve impulse transmission function

Answer 55

Proteins act as receptors of neurotransmitters during synapsis (ex: vision process starts with protein)

Question 56

Movement function

Answer 56

Muscle contraction is coordinated by two proteins: actin and myosin

Question 57

Transport function

Answer 57

Nutrients like fatty acids, vitamins, minerals, oxygen are moved through body by proteins

Question 58

What is associated with the primary level?

Answer 58

Only has chemical properties associated

Question 59

How do you disrupt the primary level?

Answer 59

Glycolysis (break amino acids apart)

Question 60

How to make more amino acids to polypeptide

Answer 60

Condensation

Question 61

What affects the primary level?

Answer 61

Condensation and hydrolysis

Question 62

What holds the secondary level together?

Answer 62

Hydrogen bonding

Question 63

Tertiary level

Answer 63

All the potential intermolecular forces and chemical bonds.

Question 64

What holds the tertiary level?

Answer 64

All chemical and physical properties (disulfide linkages, covalent bond, salt bridges, ionic bonding, hydrogen bonding, hydrophobic/hydrophilic interactions)

Question 65

What is hydrolysis?

Answer 65

Strong acid or base breaks a peptide linkage resulting in smaller peptide or amino acids. Breakups the primary structure.

Question 66

Denaturation

Answer 66

Breaking secondary, tertiary, or quaternary folding into what it wants.