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GE-CHEM > Finals: Proteins > Flashcards

Finals: Proteins Flashcards

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1
Q

naturally occuring, unbranched polymer in which the monomeric units are amino acids

A

proteins

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2
Q

all proteins contain elements ?

A

carbon, hydrogen, oxygen and nitrogen most also contain sulfur.

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3
Q

the presence of ______ sets them apart from carbohydrates and lipids, which most often do not contain ____

A

nitrogen

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4
Q

the main of protein of milk - which contains ____

A

Casein , phosphorus

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5
Q

amino acids found in proteins

A

a-amino acid

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5
Q

R group

A
  1. amino acid side chain
  2. distinguishes a-amino acids from each other
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5
Q

an organic compound that contains both amino

A

NH2 group and carboxyl (-COOH) Group

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6
Q

has non polar side chain

A

non polar amino acid

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7
Q

hydrophobic (water fearing)

A

non-polar amino acid

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7
Q

found in the interior of proteins, where their is limited contact with water

A

non-polar amino acid

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8
Q

R group - hydrocarbons (aliphatic or aromatic )

A

non polar amino acid

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9
Q

has polar side chain

A

polar amino acid

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10
Q

hydrophilic (water loving)

A

polar amino acid

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11
Q

found on the surfaces of proteins

A

polar amino acid

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12
Q

Polar amino acids are subcategorized to:

A
  1. polar neutral
  2. polar acidic
  3. polar basic
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13
Q

why are standard amino acids named that way

A

commonly encountered in proteins

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14
Q

R group consists of aliphatic:

A

alkanes, alkenes, alkynes

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15
Q

Polar neutral: At physiological pH, R group is neither?a

A

acidic nor basic

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15
Q

polar amino acids:

contains polar but NEUTRAL SIDE CHAIN

A

Polar neutral

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16
Q

side chain of polar neutral has groups that contain?

A

heteroatom

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17
Q

Polar neutral: R group can

A

hydrogen bond with water

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18
Q

for polar neutral, can it exhibit hydrogen bonding

A

yes

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19
Q

contains a carboxylc group as part of the side chains

A

polar acidic

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20
Q

side chain of polar acidic:

A

carboxylic acid

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21
Q

Polar acidic: physiological pH, R group bears a

A

negative charge, the side chain carboxyl group has lost its acidic hydrogen atom

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22
Q

contains an amino group as a part of the side chain

A

polar basic

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23
Q

side chain of polar basic

A

amine, imine

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24
Q

polar basic: at physiological pH, R group bears

A

negative charge, the side chain carboxyl group has accepted a proton

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25
Q

amino acids are linked together by an ?

A

amide (peptide) bond via a condensation reaction

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26
Q

Structure of proteins: Primary (1)

A

amino acid sequence (how many? which ones?, arrangement)

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27
Q

structure of proteins: secondary (2 degrees)

A

H-bonds on proteins backbone (how structures are stabilized)

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28
Q

Structure of proteins: Tertiary (3 degrees)

A

overall 3D shape of folded protein (overall 3d shape of a folded)

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29
Q

Structure of protein: Quarternary (4 degrees)

A

subunit organization (how polypeptides are assembled in a complex structure)

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30
Q

every protein has its own unique amino acid sequence

A

primary structure

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31
Q

It is the order sequence in which amino acids are linked together in a protein

A

primary structure

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32
Q

amino acids are linked to each other by peptide bonds

A

primary structure

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33
Q

arrangement in space adopted by the hydrogen-bonded arrangement of the backbone portion of a protein

A

secondary structure (2 degrees)

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34
Q

folding is stablizied by noncovalent interactions (specifically H bonds)

A

secondary structure

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35
Q

Beta sheets

A
  1. 2 or mroe polypeptide chains
  2. H-bonds are between adjacent strands
  3. R-groups are on opposite faces of the sheet
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35
Q

Alpha Helix

A
  1. has 1 polypeptide chain
  2. H bonds are within a single polypeptide chain
  3. R-groups are outside
  4. right handed or clockwise, spiral
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36
Q

secondary structure: A single protein chain adopts a shape that resembles a coiled spring

A

alpha-helix structure

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36
Q

secondary structure: Hydrogen bonds between C=0 and N- H entities are orientated parallel to the axis of the helix
* All of the amino acid R groups extend outward from the spiral

A

alpha helix structure

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37
Q

secondary structure: Coil configuration maintained by hydrogen bonds

A

alpha -helix structure

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38
Q

secondary: Two fully extended protein chain segments in the same or different molecules

  • Held together by hydrogen bonds.
    H-bonding between chains - Inter and/or intramolecular.
A

beta-pleated sheet structure

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39
Q

Overall three-dimensional shape of a protein.

  • Results from the interactions between amino acid side chains (R groups) that are widely separated
    trom each other.
  • hydrophobic residues cluster in the core
  • polar residues in helices and sheets
A

Tertiary structure

40
Q

Tertiary structure: 2 main factors for folding of a protein

A

1, hydrophobic residues cluster in the core
2. polar residues in helices and sheets

41
Q

Amino acids are linked together by an?

A

amide (peptide) bond via a condensation reaction

42
Q

The carboxyl group of one amino acid
interacts with?

A

with the amino group of the other amino acid.

43
Q

What are the products when a carboxyl group of one amino acid interacts with the amino group of the other amino acid?

A

molecule of water and a molecule containing the 2 amino acids linked by an amine bond

44
Q

It is when all peptide bonds are broken, and the only products are amino acids

A

complete hydrolysis

45
Q

It is when some but not all peptide bonds are broken, and the product is a mixture of amino acids and small peptides

A

partial hydrolysis

46
Q

Partial or complete disorganization of a protein’s characteristic three- dimensional shape

A

Protein Denaturation

47
Q

what are the common proteins in the body?

A

fibrous and globular

48
Q

type of protein:

Filamentous or elongated shape

A

FIBROUS PROTEIN

49
Q

type of protein:

Function is mostly structural
(strength/support)

A

fibrous protein

50
Q

type of protein:

Repetitive AA sequence
o Have a single type of secondary structures
o Simple, regular, linear structures

A

fibrous protein

51
Q

type of protein:

Usually water-insoluble
· Examples; alpha-keratin and collagen

A
52
Q

what type of protein are these ·alpha-keratin and collagen

A

fibrous protein

53
Q

fibrous protein:

α-Keratin

A

provides protective coating for organisms

54
Q

Mainly made of hydrophobic amino acid residues

A

a-Keratin

55
Q

type of fibrous protein:

Most abundant protein in humans (30% of total body protein)
* Major structural material in tendons, ligaments, blood vessels, and skin

A

collagen

56
Q

predominant structure of collagen

A

Triple-helix Glycine and proline help maintain the structure of the triple-helix

57
Q

Organic component of bones and teeth

A

collagen

58
Q

Protein classification:

  1. Spherical or globular shape
  2. Function is mostly as catalyst, transport, etc.
A
59
Q

Protein classification:

irregular AA sequence

A

globular

59
Q

Protein classification:

Usually, water-soluble
*Hydrophobic aa residues are in the protein
core

A

globular

59
Q

Protein classification:

Function is mostly as catalyst, transport, etc.

A

globular

60
Q

type of globular protein:

Oxygen-storage molecule in muscles

A

myoglobin

60
Q

examples of globular protein

A

hemoglobin and myoglobin

61
Q

type of globular protein:

Monomer
– Consists of a single peptide chain and one heme unit
– One molecule carries one O2 molecule

A

myglobin

62
Q

Has a higher affinity for oxygen than hemoglobin

A

myglobin

63
Q

Oxygen stored in myoglobin molecules serves as a ?

A

reserve source for working muscles when oxygen demand exceeds its supply

64
Q

An oxygen-carrier molecule in blood

–Transports oxygen from lungs to tissues

A

hemoglobin

64
Q

Hemoglobin: Iron atom in ??? interacts with ???

A

heme with oxygen

65
Q

a compound, usually a PROTEIN, that acts as a CATALYST for a biochemical reaction.

A

enzyme

66
Q

Most enzymes are

A

globular proteins

66
Q

Enzymes are neither

A

consumed nor permanently altered after the reaction

67
Q

enzymes undergo all the reactions of proteins including ?

A

denaturation.

68
Q

enzymes are highly?

A

efficient, specific and can be regulated

68
Q

enzyme composed only of protein (amino acid chains)

A
  • Simple enzyme
69
Q

enzyme that has a nonprotein and protein parts

A

conjugated enzyme

69
Q

Classes of enzymes:

Redox reactions

A

Oxidoreductase

70
Q

Classes of enzymes:

Transfer of functional groups

A

Transferase

71
Q

Classes of enzymes:

Hydrolysis reactions

A

Hydrolase

72
Q

Classes of enzymes:
Isomerization

A

Isomerase

72
Q

Classes of enzymes:

Addition of groups to double bonds or Removal of groups to form double bonds

A

Lyase

73
Q

Classes of enzymes:
Joining of two molecules (hydrolysis of ATP as energy source)

A

Ligase

73
Q

an enzyme that catalyzes an oxidation- reduction reaction.

A

OXIDOREDUCTASE

74
Q

an enzyme that catalyzes the transfer of a functional group from one molecule to another.

A

Transferase

74
Q

It oxidases, Reductases, Dehydrogenases

A

Oxidoreductase

75
Q

help disposal of nitrogen during the metabolism of amino acids for energy production or for synthesis of bioactive compounds from

A

Aminotransferases

75
Q

an enzyme that catalyzes a hydrolysis reaction in which the addition of a water molecule to a bond causes the bond to break.

A

. HYDROLASE:

76
Q

effect the breaking of glycosidic bonds in oligo- and polysaccharides,

A

Carbohydrases

77
Q

effect the breaking of peptide linkages in proteins,

A

Proteases

77
Q

effect the breaking of ester linkages in
triacylglycerols.

A

Lipases

78
Q

an enzyme that catalyzes addition or removal of atoms across a double bond

A

LYASE

78
Q

adds water across the double bond in
trans-Enoyl CoA during the oxidation of fatty acids for biochemical energy production

A

Enoyl CoA hydratase

79
Q

small part of an enzyme’s structure that is involved in catalysis; it is where the substrate binds to the enzyme.

A

Active Site

80
Q

formed due to folding and bending of the protein.

A

Active Site

81
Q

location in the enzyme

A

“CREVICE-LIKE”

81
Q

contains catalytic amino acid residues or groups.

A

active site

82
Q

Increasing temperature will

A

increase reaction rate

82
Q

is the temperature where maximum activity is observed

A

Optimum temperature

83
Q

Enzymes are sensitive to the?

A

acidity and basicity of their chemical environment

83
Q

Going beyond the optimum temperature will

A

destroy the enzyme structure

84
Q

is the pH where maximum activity is observed

A

Optimum pH

84
Q

Putting enzymes anywhere lower or higher the optimum pH will ?

A

destroy the enzymes structure

85
Q

in the body is usually physiological pH, but exceptions are proteolytic enzymes in the stomach (pH ~2)

A

optimun pH

85
Q

are the reactants for enzyme- catalyzed reactions

A

Substrates

86
Q

is the maximum amount of substrate molecules that an enzyme can convert to products

A

Turnover number

86
Q

When an enzyme is saturated, its activity reaches a

A

plateau

87
Q

Changes in enzyme concentration are directly proportional to enzyme activity

A

Enzyme Concentration

GE-CHEM (5 decks)

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