Chem 111 - Proteins

Front 1

Proteins are molecules that controls every human activity including

Back 1

1. digestion
2. buildup of body muscles
3. movement
4. helps breathing transport of oxygen

Front 2

Proteins _____ contain the genetic code

Back 2

Proteins do not contain the genetic code

Front 3

Proteins are made of amino acid and the nature and function of a protein is dependent upon how the amino acids is arranged in a _____ (i.e.) the sequence of the amino acid arrangement.

Back 3

Proteins are made of amino acid and the nature and function of a protein is dependent upon how the amino acids is arranged in a protein molecule (i.e.) the sequence of the amino acid arrangement.

Front 4

Proteins are not an energy source only about ___% of human energy is derived from a protein.

Back 4

Proteins are not an energy source only about 10% of human energy is derived from a protein.

Front 5

Out of 100s of amino acids, only ___ amino acids, participate in making a protein.

Back 5

Out of 100s of amino acids, only 20 amino acids, participate in making a protein.

Front 6

What is the molecular weight of proteins?

Back 6

40 MM proteins

Front 7

Amino acids exist as _____ (i.e.) contain positive and negative charge

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Amino acids exist as zwitter ions (i.e.) contain positive and negative charge

Front 8

Amino acids are _____ (i.e.) contain both an acid and a base

Back 8

Amino acids are amphoteric molecules (i.e.) contain both an acid and a base

Front 9

All the 20 amino acids are the same except the _____

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All the 20 amino acids are the same except the "R" side chain

Front 10

Types of amino acids

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1. neutral nonpolar (9)
2. neutral polar (6)
3. acidic amino acids (2)
4. basic amino acids (3)

Front 11

The net charge of an amino acid is _____

Back 11

zero

Front 12

The pH, which is the amino acid, have a net charge of zero it is _____

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isoelectric point (PI)

Front 13

At a pH less than the PI (isoelectric point), the net charge of an amino acid is _____

Back 13

(+1)

Front 14

At a pH higher than the PH (isoelectric point), the net charge of an amino acid is _____

Back 14

(-1)

Front 15

Essential Amino Acids

Back 15

• only obtained from diet (e.g. meat, eggs, milk, soy products)
• not synthesized in humans
• proteins that provide all the essential amino acids are known as complete or adequate proteins. Diet that lacks are in complete proteins.

Front 16

Corn does not contain

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TRP and LYS

Front 17

Nonessential Amino Acids

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• synthesized in humans from the essential amino acids which are obtained from the diet

Front 18

Rice contains _____ & _____ but not _____

Back 18

Rice contains MET & TRP but not LYSINE

Front 19

Beans contain _____

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lysine

Front 20

Rice + Beans →

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complementary proteins

Front 21

Amino acids combine together to lose water to result in amide known as _____

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Amino acids combine together to lose water to result in amide known as peptides

Front 22

"N" terminis

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is always at the left end of the peptide

Front 23

"C" terminis

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is always at the right end

Front 24

2 amino acids is a ______

Back 24

dipeptide

Front 25

3 amino acids is a _____

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tripeptide

Front 26

4-10 amino acids is a _____

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oligopeptide

Front 27

11-49 amino acids is a _____

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polypeptide

Front 28

50 & ↑ amino acids is a _____

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protein

Front 29

_____ or _____ produced in the brain
appetite enhancing peptide → obesity peptide

Back 29

Neuropeptide y or galantine produced in the brain appetite enhancing peptide → obesity peptide

Front 30

_____ is an appetite inhibiting peptide

Back 30

Cholecystakonin is an appetite inhibiting peptide

Front 31

_____ is a 9 amino acid oligopeptide regulates blood pressure

Back 31

Vasopressin is a 9 amino acid oligopeptide regulates blood pressure

Front 32

Oxytocin (Pytocin) is a 9 amino acid oligopeptide produced in the uterus

Back 32

1. enhancing or stimulates the uterus contraction during childbirth
2. stimulate mammary gland during lactation
3. enhances maternal characteristics

Front 33

Vasopressing and oxytocin are produced in the

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pituitary glands

Front 34

Feel good or pain relieving peptides are _____ and _____

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Met-enkhaphalin and Leu-enkhaphalin (natural endorphins)

Front 35

Structure of Met-enkhaphalin

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TYR.GLY.PHE.PHE.MET

Front 36

Structure of Leu-enkhaphalin

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TYR.GLY.PHE.PHE.LEU

Front 37

A pain enhancing peptide is

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Bradykinin (9 amino acid oligopeptide)

Front 38

What are globular proteins?

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• enzymes are globular proteins
• helps digest food of the diet

Front 39

What are structural proteins?

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• Fibrous proteins (ex: nail, hair, hooves, & skin contain keratinized)

Front 40

What are defense proteins?

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• prevents blood clot in the arteries and thus prevent athlerosclerosis
• interferon - defends the immune system
• snake venom

Front 41

What are transport proteins?

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• hemoglobin transports oxygen
• lipoproteins

LDL, HDL, and VLDL are all transport cholesterol triglycerides

Front 42

What are movement proteins?

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• muscles, tissues, help etc.

Front 43

What are structural proteins?

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• bone, skin, cartilage, tendon & collagen is skin

Front 44

What are storage proteins?

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• casein in milk
• egg yolk

Front 45

What are stress response proteins?

Back 45

• cytochome (check page 450)
• metallothionein → "cysteinerich metallothionein"

Front 46

What are the different structures of proteins?

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• primary structure
• secondary structure
• tertiary structure
• quarternary structure
• Allosteric Protein structure

Front 47

Primary Structure

Back 47

means or reveals that amino acid sequence of arrangement is a protein. The function and the nature of the protein is dependent on how the amino acid are arranged. The sequence of the amino acid arrangement can not be mutated or altered. Even a small alteration will drastically affect the function of a protein.

E.g. hemoglobin, a protein present in the blood is made of four biologically active peptide molecules

Front 48

Oxygen carrier

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VAL.HIS.LEU.THR.PRO.GLU.GLU.LYS

oxygen carrier

Front 49

Sickle cell carrier

Back 49

VAL.HIS.LEU.THR.PRO.VAL.GLU.LYS

sickle cell carrier

Front 50

One change in an amino acid alters the _____ of the protein

Back 50

One change in an amino acid alters the function of the protein

Front 51

Insulin is made up of peptide molecule chain

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A (21 amino acids) & B (30 amino acids)

Front 52

INSULIN
Chains A & B are intermolecularly connected by two disulfide linkages between two _____ amino acids

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INSULIN
Chains A & B are intermolecularly connected by two disulfide linkages between two cysteine amino acids

Front 53

Chain A of insulin contains an intermolecular ____ linkage

Back 53

Chain A of insulin contains an intermolecular disulfide linkage

Front 54

_____ is essential for metabolizing glucose

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Insulin is essential for metabolizing glucose

Front 55

Type ___ diabetes is due to absence or inability to produce insulin

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Type 1 diabetes is due to absence or inability to produce insulin

Front 56

Type ___ diabetes is due to inadequate protection of biosynthetic insulin and; it is a "lifestyle disease"

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Type 2 diabetes is due to inadequate protection of biosynthetic insulin and; it is a "lifestyle disease"

Front 57

Ingestion of insulin inhibits _____ insulin

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Ingestion of insulin inhibits biosynthetic insulin

Front 58

What is the source of insulin?

Back 58

traditionally harvested from animal pancreas currently obtained genetic engineered insulin

Front 59

What is myoglobin?

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a 153 amino acid, single strand protein GLY .... GLY carries O₂ to the muscles tissues and stores in the muscles and helps endurance

Front 60

What is the structure of oxytocin?

Back 60

AAAAA

Front 61

Secondary Structure of Proteins

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refers to the spatial arrangement of amino within the primary structure (i.e. hydrogen bonding) within the primary structure

Front 62

What are the three kinds of secondary structures?

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1. alpha helix
2. B pleated
3. Triple helix

Front 63

alpha (α) helix

Back 63

proteins like nails, hair, hooves, collagen, keratin contain alpha helix structure

• a single strand protein is coiled like a rod with right handed confirmation containing hydrogen bonding between hydrogen of the amino group and the oxygen of the carbonyl group (C=O) of amino acids remotely, This results in the strength of the above proteins

Front 64

β pleated

Back 64

• fibroin and silk
• two or more strands of biologically active peptide molecules arranged side by side. Fully extended (not coiled) like a ladder containing collinear hydrogen bonding between the amino acids parallel β-pleated (i.e. arranged in the same order)

(i.e. coliner hydrogen increases the anti-parallel β-pleated)

Front 65

Triple helix

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• present in cartilage, tendon, bone, etc
• 3 strands of proteins are coiled or woven like a braid

Front 66

Tertiary Structures of Proteins refers to

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refers to the 3-dimensional conformations assumed by proteins; and this known as native configuration or natural confirmation. The natural and function of a protein depends upon the side chain interactions of various amino acids in the single strand proteins the chain interactions

Front 67

TERTIARY STRUCTURES OF PROTEINS
_____ interaction is the interaction between the neutral nonpolar groups

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Hydrophobic interaction is the interaction between the neutral nonpolar groups

Front 68

TERTIARY STRUCTURES OF PROTEINS
_____ interaction: interaction between neutral polar [OH] groups

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Hydrophobic interaction: interaction between neutral polar [OH] groups

Front 69

TERTIARY STRUCTURES OF PROTEINS
_____ bonding interaction between neutral polar groups

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Hydrogen bonding interaction between neutral polar groups

Front 70

TERTIARY STRUCTURES OF PROTEINS
_____ or _____ or electrostatic interaction

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Ionic or salt bridge or electrostatic interaction

Front 71

TERTIARY STRUCTURES OF PROTEINS

LYS .... LYS
Disulfide linkage or covalent bonding

Back 71

Disulfide linkage or covalent bonding

Front 72

Tertiary Structure (i.e.) R-group interaction in a single strand proteins occur in between the amino acids: and it is present in globular proteins known and "enzyme" (i.e.) intramolecular R-group interactions are present in the enzymes

Back 72

Tertiary Structure (i.e.) R-group interaction in a single strand proteins occur in between the amino acids: and it is present in globular proteins known and "enzyme" (i.e.) intramolecular R-group interactions are present in the enzymes

Front 73

Quarternary Structures of proteins contain the same ....... present in the tertiary structures.

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1. hydrophobic
2. hydrophilic
3. hydrogen bonding
4. electrostatic

Front 74

The side chain interactions in the quaternary structures are intermolecular (i.e.) ...

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the R-group interact in between the peptide molecules

Front 75

Quarternary structures are present in the ____ proteins (i.e.)

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Quarternary structures are present in the oligo proteins (i.e.) proteins containing two or more biologically active proteins molecules

Front 76

Hemoglobin

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an O₂ carrier contains four biologically active peptide molecules and hence exhibit a quaternary structure

Front 77

denaturation or destruction of the active proteins

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If proteins are subjected to two conditions that would destroy the side chain interactions present in the tertiary & quaternary protein structures and the hydrogen bonding

Front 78

Denaturation of proteins does not affect the _____ structure

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Denaturation of proteins does not affect the primary structure

Front 79

Heat destroys the _____ and _____ bonding

Back 79

Heat destroys the hydrophobic & hydrogen bonding

Front 80

Alcohol destroys _____ and _____ but not water

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Alcohol destroys hydrogen bonding and hydrophobic interaction but not water

Front 81

Strong acids and bases destroy the ionic and hydrogen bonding salt bridge

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Strong acids and bases destroy the _____ and _____ _____ _____ ____

Front 82

Mechanical stress destroys the _____

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Mechanical stress destroys the hydrophobic interaction

Front 83

Heavy metals including Ag, Pb, and Hg destroy the _____ _____ and _____ _____.

Back 83

Heavy metals including Ag, Pb, and Hg destroy the ionic bonding and disulfide linkage.

Front 84

Disulfides are produced by _____ [reducing agent]

Back 84

Disulfides are produced by Mercaptoethanol [reducing agent]

Front 85

What are vitamins?

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• water soluble "coenzymes"
• water insoluble "health food"

Front 86

What are enzymes?

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are known as biological catalysts; that increase the biochemical reactions in the tissue cells by reducing the activation energy

Front 87

lactose →(lactase)

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β-d-galactose & α-d-glucose

Front 88

sucrose →(sucrase)

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β-d-fructose & α-d-glucose

Front 89

triglycerides →(lipase)

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glycerol & fatty acids

Front 90

protein →1. pepsin 2. trypsin

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amino acids

Front 91

Enzymes are very specific in the activity; and the substrate binds to a site known as the "_____ _____" thru their side chain interactions and them metabolizes

Back 91

Enzymes are very specific in the activity; and the substrate binds to a site known as the "active site" thru their side chain interactions and them metabolizes

Front 92

The shape of the active site of an enzyme is the _____ the substrate so they can bind effectively.

Back 92

The shape of the active site of an enzyme is the same as the substrate so they can bind effectively.

Front 93

The shapes of the active site of an enzyme and the substrate is like a "____ ____ ____" model

Back 93

The shapes of the active site of an enzyme and the substrate is like a "lock and key" model

Front 94

The lock and key model is known as a ______

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fixed model

Front 95

In certain cases: Induced fit model enzymes adjust their shape to accommodate the substrate and the substrate in turn adjusts its shape to fit into the active site, and when the biochemical reactions are complete both enzymes and substrates regain the original shape.

Back 95

In certain cases: Induced fit model enzymes adjust their shape to accommodate the substrate and the substrate in turn adjusts its shape to fit into the active site, and when the biochemical reactions are complete both enzymes and substrates regain the original shape.