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Pbio Prelims > Proteins Part 3 > Flashcards

Proteins Part 3 Flashcards

1
Q

Types of conjugated proteins

A

Hemoproteins
Lipoproteins
Glycoproteins
Phosphoproteins
Nucleoproteins
Metalloproteins

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2
Q

Heme unit

Hemoglobin
Myoglobin

A

Hemoproteins

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3
Q

Lipid
Low-density lipoprotein LDL
High density lipoprotein HDL

A

Lipoproteins

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4
Q

Carbohydrates

Gamma globulin
Mucin
Interferon

A

Glycoproteins

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5
Q

Phosphate group
Glycogen phosphorylase

A

Phosphoproteins

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6
Q

Nucleic acid
Ribosomes
Viruses

A

Nucleoproteins

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7
Q

Metal ions
Iron-ferritin
Zinc-alcohol dehydrogenase

A

Metalloproteins

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8
Q

Functions of hemoproteins

A

Carrier of O2 in blood
Oxygen binder in muscles

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9
Q

Function of lipoproteins

A

Lipid carrier

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10
Q

Functions of
Gamma globulin
Mucin
Interferon

A

Antibody
Lubricant in mucous secretions
Antiviral protection

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11
Q

Function of
Glycogen phosphorylase

A

Enzyme in glycogen
Phosphorylation

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12
Q

Functions of
Ribosomes
Viruses

A

Site for protein synthesis in cells
Self replicating, infectious complex

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13
Q

Functions of
Ferritin
Alcohol dehydrogenase

A

Storage complex for iron
Enzyme in alcohol oxidation

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14
Q

Four types of structures in proteins

A

Primary
Secondary
Tertiary
Quarternary

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15
Q

The order in which amino acids are linked together in a protein

A

Primary structure

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16
Q

Complete the sentence

Every protein has its

A

Own unique amino acid sequence

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17
Q

Who sequenced and determined the primary structure for the first protein-insulin

A

Frederick sanger
1918-2013

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18
Q

No pattern no twists merely sequence by peptide bond

A

Cis-trans isomerism

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19
Q

preffered orientation

A

Trans isomer

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20
Q

Humulin

A

1st genetically approved protein
B y eli-lilly

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21
Q

A single protein chain adopts a shape that resembles a coiled spring
H bonding between same a.a -intramolecular
Coiled helical spring
R group outside of the helix

A

Alpha helix a-helix

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22
Q

H bonding between 2 different chains inter/intra
Side chains below or above

A

Beta-pleated sheets

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23
Q

Is a protein structure that is neither an helix nor a b-pleated sheet

A

Unstructured protein segment

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24
Q

Four types of interactions

A

Disulfide
Electrostatic
H-bonding
Hydrophobic interactions

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25
Q

Covalent, strongest between two cysteine groups has Sulfur

A

Disulfide bond

26
Q

AKA salt bridge between charged side chains of acidic R and basic R amino acids

A

Electrostatic interactions

27
Q

Weak bond between polar acidic and or basic R groups

A

H-bonding

28
Q

Between non polar side chains

A

Hydrophobic interactions

29
Q

Multimeric proteinb
Highest level of protein org
2 or more polypeptide chains (subunits)
Not covalently bonded
Refferd to as oligomeric proteins
Contain even number of subunits

A

Quaternary structure of proteins

30
Q

Elongated shape
Simple regular linear structures single type of secondary structure
Insoluble in water

A

Fibrous proteins

31
Q

Function of fibrous proteins

A

Aggregate together to form macromolecular structures/ hair nails

Structural provide support and external protection

32
Q

Examples of fibrous proteins

A

Keratin
Collagen
Elastin
Myosin
Fibrin

33
Q

Occurence and functions of
Keratins
Collagens
Elastins
Myosins
Fibrin

A

Keratins-found in wool feathers hooves silk and fingernails
Collagens-found in tendons bone and other connective tussue
Elastins-found in blood vessels and ligaments
Fibrin-found in blood clots

34
Q

Most abundant proteins in humans 30%
Structure of tendons, ligaments,blood vessels and skin
Organic component of bones and teeth
Triple helix
Glycine 1/3 proline 1/3

A

Collagen

35
Q

Spherical or globular shapes (several types of secondary structure)
Generally water soluble hydrophobic amino acids residues in the protein core

A

Globular protein

36
Q

Uses/functions of globular protein

A

Signaling molecules

Metabolic chemistry
Catalysis transport and regulation

37
Q

Globular proteins
Insulin
Myoglobin
Hemoglobin
Transferrin
Immunoglobulin

A

Insulin-regulatory hormone for controlling glucose
Myoglobin-involved in oxygen storage muscles
Hemoglobin-involved in oxygen transport in blood
Transferrin-involved in iron transport in blood
Immunoglobulins- involved in immune system responses

38
Q

An oxygen storage molecule in muscles
Monomer-single peptide chain with one heme unit
Binds one o2 molecule
Reserve oxygen source for working muscles

A

Myoglobin

39
Q

Carrier molecule in blood
Transports oxygen from lungs to tissues
Tetramer (4 peptide chains)
Transport up to 4 oxygen molecules at a time
Iron atom in heme interacts with oxygen

A

Hemoglobin

40
Q

Associated with cell membranes
Insoluble in water

A

Membrane protein

41
Q

Use/function membrane protein

A

Transport of molecules across the cell membrane

42
Q

Proteins play crucial roles in

A

Most biochemical processes

43
Q

Functional versatility of proteins stem from

A

Ability to bind small molecules specifically and strongly
Ability to bind other proteins and form fiber like structures
Ability to integrated into cell membranes

44
Q

Proteins based on fuctions
-Enzymes are best known for their catalytic role

A

Catalytic proteins

45
Q

Proteins based on fuctions

Aka immunoglobulin or antibodies
Immune system

A

Defense proteins

46
Q

Bind small biomolecule like oxygen and other ligands and transport them to other locations in the body

A

Transport proteins

47
Q

Transmit signals to coordinate biochemical processes

A

Messenger protein

48
Q

Regulate carbohydrate metabolism

A

Insulin and glucagon

49
Q

Regulate body growth

A

Human growth hormone

50
Q

Necessay for all forms of movement ( contraction)
Actin-and myosin
Movement of sperm-needs protein long flagella

A

Contractile protein

51
Q

Confer stiffness and rigidity
Collagen part of cartilage
A-keratin

A

Structural proteins

52
Q

Span a cell membrane control the movement of small molecules and ions

A

Transmembrane proteins

53
Q

Bind and store small molecules
Ferritin- an iron storage protein
Myoglobin- an oxygen storage protein present in muscle

A

Storage proteins

54
Q

Bind and initiate the effect it carries
Bind to enyzmes to turn on and off thus regulating

A

Regulatory protein

55
Q

Important in the early stages of life
Casein milk and ovalalbumin egg white

A

Nutrient proteins

56
Q

Acid base balance within the body

A

Buffer proteins

57
Q

Maintain fluid balance

A

Fluid balance protein

58
Q

Reverse or breakage of peptide bond

A

Hydrolysis of proteins

59
Q

All peptide bonds are broken

A

Complete protein hydrolysis

60
Q

Some but not all peptide bonds are broken

A

Partial protein hydrolysis

61
Q

Tertiarty to primary
Quarternary to primary
Secondary to primary

A

Protein denaturation

62
Q

Reconstruction of a protein to their original form especially after denaturation

A

Protein renaturation

Pbio Prelims (11 decks)

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