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BIOCHEM > PROTEINS > Flashcards

PROTEINS Flashcards

1
Q

greek word of PROTEIN

A

PROTEIOS “primary or of first importance”

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2
Q

most important food group

A

Proteins

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3
Q

they play key roles in constructing ang maintaining living cells.

A

Proteins

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4
Q

function of proteins Bio

A

biological and chemical catalysts (enzymes)

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5
Q

function of proteins For me

A

For metabolic regulation (as hormones)

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6
Q

function of proteins For de

A

For defense (as anti-bodies)

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7
Q

function of proteins t

A

transport of oxygen

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8
Q

function of proteins s

A

storage

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9
Q

function of proteins pro

A

provide structure to the body of a multi-celled organism

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10
Q

function of proteins bui

A

building of new tissues and maintaining tissues that are developed

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11
Q

function of proteins for mu

A

for muscle contraction

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12
Q

compositions of proteins

A

polypeptides + (co-factors, co-enzymes, prosthetic groups)

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13
Q

polypeptides + (co-factors, co-enzymes, prosthetic groups)

A

covalently linked a-amino acids

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14
Q

non-amino acid components (metal ions)

A

co-factors

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15
Q

organic co-factors (nucleotides)

A

co-enzymes

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16
Q

covalently attached co-factors

A

prosthetic groups

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17
Q

UNLKE FATS AND CARBS, PROTEINS ARE NOT STORED

A

TRUE

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18
Q

giant polymers whose molecular masses range from thousands to millions.

A

polymers of amino acid

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19
Q

elementary composition of protein

A 
55% carbon
7% hydrogen
23% oxygen
16% nitrogen
1% sulfur
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20
Q

structure of proteins

refers to the NUMBER, SEQUENCE, and KIND of amino acids linked by PEPTIDE BONDS (LINEAR STRUCTURE)

A

PRIMARY LEVEL

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21
Q

bond responsible for primary level

A

peptide bond

22
Q

peptide bond can be broken by

A

acid or base hydrolysis

23
Q

refers to a regular geometric pattern along a polypeptide (H-bonding)

A

Secondary level of structure

24
Q

regularly repeated 3D shape of the molecule

A

secondary level

25
Q

3 kind of secondary level structure

A 
Alpha Helix
Pleated Sheets
 -parallel
 -anti-parallel
Collagen Superhelix
26
Q

composed of peptide chains arranged side by side resembling paper folded into pleats

A

Pleated Sheets (Beta-conformation)

27
Q

Regions of peptide chains coiled into a spiral shape

A

Alpha Helix

28
Q

composed of a series of chains that have all of the N-terminals at one end

A

Parallel

29
Q

Every other chain points to the opposite direction (alternating C and N terminals)

A

Anti-parallel

30
Q

it has triple helix protein

A

Collagen superhelix

31
Q

a combination of primary, secondary, and R-groups interacting wherein COILING AND FOLDING take place in the structure

A

tertiary level

32
Q

tertiary level (appearance)

A

complex and globular shape structure

33
Q

tertiary structures are stabilized by the ff interactions

A 
additional H-bonds
ionic bonds or salt bridges
pi-pi complexation
hydrophobic interactions of non-polar side chains
disulfide linkages
34
Q

consists of several polypeptide chains NOT covalently linked to each other

A

quaternary level

35
Q

they have fixed ratios, fixed masses, and form definite geometric structures

A

quaternary level

36
Q

shows the arrangements of subunits in 3D and SUPERFOLDING TAKES PLACE

A

quaternary level

37
Q

a change in the secondary, tertiary and quaternary structure of proteins

A

denaturation

38
Q

occurs when a NATIVE PROTEIN UNFOLDS when WEAK BONDS ARE DISRUPTED

A

denaturation

39
Q

Proteins are EASILY DENATURED AND MAY OR MAY NOT BE REVERSIBLE

A

TRUEEE

40
Q

REVERSE DENATURATION

A

renaturation

41
Q

causes loss of biological activity

A

denaturation

42
Q

Protein denaturants:

A 
Heat
Organic solvents
Acids and Bases
Heavy metals (Pb, Ag, Hg)
Alkaloidal Rgts (Tannic acid)
Extreme pH
Reducing agent
Radiation
43
Q

Heat

A

motion of molecules

disrupts H-bonds

44
Q

Organic solvents (ETHER AND ALCOHOL) - affects

A

protein solubility & coagulation of protein

disrupts H-bonds

45
Q

Acids and Bases

A

H-bonds

Prolonged contact will hydrolize proteins

46
Q

Heavy metals (Pb, Ag, Hg)

A

salt bridges

disulfide

47
Q

Alkaloidal rgts (tannic acid)

A

disrupts salt bridges and precipitates proteins

48
Q

Extreme pH

A

hydrogen and ionic bonds

49
Q

Reducing agent

A

disrupts disulfide bonds

50
Q

Radiation

effects

A

motion of molecules

disrupts H-bonds

BIOCHEM (3 decks)

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