Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

BMSC 200 > post midterm ch. 6-10 > Flashcards

post midterm ch. 6-10 Flashcards

1
Q

what is vitalism?

A

the belief that living things are fundamentally different from non living things

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what is an apoenzyme?

A

inactive protein portion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what is a cofactor/conenzyme?

A

active non protein portion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what is a holoenzyme?

A

active whole enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what do catalysts do?

A

lower the amount of energy required for a reaction to proceed, speed up attainment of equilibrium, unchanged by the reaction and recycled to participate in another reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

what is an active site?

A

3D cleft formed from different parts of the polypeptide chain, where substrates are bound to enzymes by multiple weak interactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

when is a reaction spontaneous (exergonic)?

A

only if delta G is negative

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

what does the delta G of a reaction depend on?

A

the free energy of the product minus the free energy of the reactants

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what is the relationship between the rate of a reaction and the activation energy?

A

inverse and exponential

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

when enzymes provide a lower energy pathway between the substrate and the product what happens?

A

activation energy of the transition state decreases which increases the rate of the reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what are the forces that lower the activation energy?

A
  • binding effects (substrate binding and transition state stabilization)
  • chemical effects (acid/base catalysis and covalent catalysis)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

binding of substrate in the active site provides what?

A

specificity and catalytic power

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

how does substrate binding promote reactions?

A
  • reduces entropy
  • alignment of reactive functional groups of enzyme with the substrate
  • desolation of the substrate (removal of H2O molecules) to expose reactive groups
  • distortion of substances
  • induced fit of the enzyme in response to substrate binding
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Thrombin cleaves which bonds?

A

Arg-Gly bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Trypsin cleaves by ?

A

cuts beside positively charged residues, cleaves by Lys and Arg

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Chymotrypsin cleaves by ?

A

cuts beside aromatics, cleaves by Phe, Tyr, or Met

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Elastase cleaves by ?

A

cuts beside small hydrophobics, cleaves by Gly and Ala

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

what is Histidines role in the catalytic mechanism?

A

acts to accept and donate a proton at each of the 2 stages of the reaction mechanism (acid base catalysis)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

what is Aspartates role in the catalytic mechanism ?

A

stabilizes the positively charged Histidine to facilitate serine ionization

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

what is Serine’s role in the catalytic mechanism?

A

attacks the carbonyl group of the peptide bond to be cleaved (covalent catalysis)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

what is involved in regulation of enzyme availability? (long term)

A

location, rate of synthesis, and degradation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

what is involved in regulation of enzyme activity?

A
  • covalent modification (phosphorylation, methylation, glyosylation etc.)
  • non-covalent modification (allosteric regulation)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

enzymatic pathways are often controlled through what?

A

negative feedback inhibition by the final product of the pathway to inhibit the enzyme catalyzing the first unique and committed step of the branch

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

the carbon that becomes chiral as a result of cyclization is ?

A

the anomeric carbon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

what is mutarotation?

A
  • the alpha and beta configurations inter convert
  • occurs through a linear intermediate
  • represents a change in configuration
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

in solution, glucose is how much beta- glucopyranose and how much alpha-glucopyranse?

A

2/3 b-glucopyranose
1/3 a-glucopyranose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

where is b-fructopyranose found?

A

in honey, is extremely sweet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

what happens when you heat b-fructopyranose?

A

converts to b-fructofuranose, less sweet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

corn syrup has a high concentration of what and is used to sweeten what?

A

high concentration of b-fructopyranose, used to sweeten cold drinks (not hot)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

myrosinase acts on glucosinolate to produce what?

A

glucose and isothiocyanate (sharp bitter taste)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

when do myrosinase and glucosinolate come together?

A

upon tissue damage

32
Q

linear forms of monosaccharides are oxidized by what and allows for what?

A
  • oxidized by mild oxidizing agents like iron and copper
  • allows for quantifications of sugars present in blood or urine
33
Q

the end of the chain with a free anomeric carbon is called what?

A

the reducing end

34
Q

what is a glycosidic bond?

A

primary structural linkage in all polymers of monosaccharides

35
Q

where do O-glycosidic bonds occur?

A

through oxygen

36
Q

where do N-glycosidic bonds occur?

A

through nitrogen

37
Q

higher order carb structures are generated through the action of what?

A

glycotransferases

38
Q

lactose intolerant people have insufficient levels of what?

A

insufficient levels of lactase that catalyses the hydrolysis of lactose into glucose and galactose

39
Q

what are homopolysaccharides?

A

polymers containing a single type of monosaccharide

40
Q

what are heteropolysaccharides?

A

polymers containing more than one type of monosaccharide

41
Q

where and what form is glucose stored in animals?

A

stored as glycogen in the liver and skeletal muscle of animals

42
Q

what form is glucose stored in plants?

A

stored as starch, mix of amylose (unbranched) and amylopectin (branched)

43
Q

what is amylose?

A

a linear polymer of glucose residues through a(1-4) bonds

44
Q

what is amylopectin?

A

consists of a(1-4) linked glucose residues with a(1-6) branch points every 24-30 residues

45
Q

how many reducing ends do amylose and amylopectin have?

A

one

46
Q

how many non-reducing ends do amylose and amylopectin have?

A

amylose has one
amylopectin has multiple

47
Q

what is cellulose?

A
  • the primary component of plant cell walls (fibre)
  • a linear, homopolysaccharide of glucose residues
  • linear arrangement of b(1-4) glycosidic residues
48
Q

what is chitin?

A
  • the main component of exoskeletons (insects, lobsters etc.)
  • a linear homopolysaccharide of N-acetylglucosamine residues
49
Q

what is the chemical difference between cellulose and chitin?

A

the replacement of hydroxyl group at C2 with acetylated amino group

50
Q

what are glycoproteins?

A

proteins with covalently attached sugars, mostly protein, and serve a variety of biological roles

51
Q

what are proteoglycans?

A

protein component linked to a carb called glycosaminoglycan, mostly carb, and serve structural and lubricating functions

52
Q

in glycoproteins what are the sugars attached to?

A

the amide nitrogen of the side chain of asparagnine
OR
the hydroxyl oxygen of the side chain of serine or threonine

53
Q

what does erythropoietin do?

A
  • stimulates red blood cell productions, highly affective in the treatment of anemia
  • exploited by endurance athletes to increase oxygen carrying capacities
54
Q

what is the extracellular matrix (ground substance) made of and what does it do?

A
  • made of a mesh work of fibrous proteins and heteropolysaccharides (glycosaminoglycans)
  • holds cell together, provides a porous pathway for diffusion of nutrients/waste products and serves a cushioning function
55
Q

what are fatty acids?

A

hydrocarbon with carboxylic head, usually an even number of carbons (12-24)

56
Q

what does a saturated fatty acid look like?

A

no double bonds

57
Q

more carbons means what for the melting point?

A

higher melting point

58
Q

fatty acids required for energy are stored as what?

A

triacylglycerols

59
Q

what is a low oxidation state?

A

less oxygenated fuels burn more efficiently; triacylglycerols have lower oxygenation state than carbs

60
Q

what is a low hydration state?

A

lipids are hydrophobic with limited interaction with water providing a more compact, dehydrated energy storage form

61
Q

what is saponification?

A

making soap from fat- treatment of fat with a string vase breaks the water linkages to release free fatty acids

62
Q

how do fatty acids function as detergents and soaps ?

A

through formation of micelles that capture hydrophobic molecules

63
Q

what are waxes?

A

non-polar esters of long chain fatty acids and long chain mono hydroxyl is alcohols

64
Q

what are glycercophospholipids?

A

most abundant lipids in membranes, glycerol backbone with a phosphate at the C3 position

65
Q

archaebacteria (extremophiles) membrane lipids contain what?

A
  • ether linkages
  • branch points within the hydrocarbon tails
  • membrane spanning hydrocarbon tails composed from a single molecule
66
Q

what is the structure of steroids (sterols) and what do they do?

A

four fused ring steroid nucleus (3 six carbon rings and a 5 carbon D ring)
- serve as precursors for many biologically active products ex. testosterone

67
Q

what does cholesterol do?

A

serves a number of critical biological functions like mediating membrane fluidity
also serves as a precursor of steroid hormones and bile salts

68
Q

what are the active roles of lipids?

A

intracellular signaling molecules, hormones, enzyme cofactors, pigments, vitamins

69
Q

what are eicosanoids?

A

paracrine hormones, derivatives of C20 PUFAs
(prostaglandins, thromboxanes, leukotrienes)

70
Q

what are prostaglandins involved in?

A

construction of blood vessels

71
Q

what are thromboxanes involved in?

A

blood clot formation

72
Q

what are leukotrienes involved in?

A

smooth muscle contraction

73
Q

below the phase transition temp the membrane is?

A

too solid

74
Q

above the phase transition temp the membrane is?

A

too fluid

75
Q

how do peripheral membrane proteins associate with the membrane?

A

through electrostatic or H-bonding interactions

76
Q

the bulk of the peripheral membrane proteins is where?

A

in the cytosol or extracellular space

77
Q

what does a hydropathy index look at?

A

the hydrophobic characteristics of a protein to predict transmembrane regions

BMSC 200 (2 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions