Lec 9/10 Flashcards

1
Q

Atoms most abundant in biomolecules

A

H,O,S,N,P,C

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2
Q

what are basic organic compounds?

A

alcohol, aldehyde, ketone,carboxylic acid, sulfhydryl group, A disulfide, Amino group,Phosphoester, Amide

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3
Q

characteristics of noncovalent bonds

A
  • weak attractive forces
  • ionic interaction
  • form H-bonds
  • hydrophobic effect
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4
Q

characteristics of covalent bonds

A
  • strong attractive forces

- can make single, double, triple bonds

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5
Q

properties of water

A
  • polar
  • cohesive: H-bonds
  • Solvent(H-bonds, ionic interactions)
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6
Q

Basic biological compounds

A

aa, nucleotides, sugars, lipids, proteins, DNA, RNA, starch, cellulose, biomembranes

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7
Q

what is a common theme for all biological compounds?

A

loss of water in formation of covalent polymers

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8
Q

characteristics of aa

A
  • alpha C, R group, contain both acidic(carboxyl) and basic (amino)
  • at pH 7-double ionized form(amino accepted a proton–>+, carboxyl lost a proton–>-)
  • Zwitterion form of aa(equal nunber of positive and negative ions)–> net charge=0–>neutral
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9
Q

is polar molecule water soluble?

A

yes

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10
Q

is nonpolar molecule water soluble?

A

no

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11
Q

what does Amphipathic mean?

A

having both polar and non-polar properties

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12
Q

what does Aliphatic mean?

A

having a straight or branched chain structure

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13
Q

what aa are hydrophobic?

A

Alanine-A, Valine-V, Leucine-L, Isoleucine-I, Proline-P, Methionine-M, Phenylalanine-F, Tryptophan-W

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14
Q

what aa are hydrophyllic?

A

Glycine-G, Serine-S, Threonine-T, Cysteine-C, Asparagine-N, Glutamine-Q, Tyrosine-Y

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15
Q

what are aa hydrophyllic and negative charge?

A

Aspartic acid-D, Glutamic acid-E

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16
Q

what are aa hydrophyllic and positive charge?

A

Lysine-K, Arginine-R, Histidine-H

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17
Q

what are characteristics of polypeptide chains?

A
  • aa linked by peptide bonds
  • a-carboxyl group joined to a-amino group
  • peptide bond=amide bond: covalent bond
  • loss of a water molecule
  • require an input of free energy
  • stable, >1000 years in absence of catalyst
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18
Q

what is another name for aa unit?

A

residue

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19
Q

does polypeptide chain have polarity?

A
  • amino-terminal (N-terminal)

- carboxyl-terminal(C-terminal)

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20
Q

what type of bond mainly found in backbone of polypeptide chains?

A

H-bonds

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21
Q

what are characteristics of proteins?

A
  • 50% of dry weight of cell
  • catalysts
  • transport+store other molecules. EX: O2
  • mechanical support, immune protection, generate movement, transmit nerve impulses, control growth and differentiation
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22
Q

what gives function of a protein?

A

chemical reactivity of functional groups give function

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23
Q

what categories of proteins?

A

Fibrous proteins and globular proteins

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24
Q

what is fibrous protein?

A

contributes to structure of cell

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25
Q

what is globular proteins?

A

contributes to function of cell

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26
Q

what are characteristics of fibrous protein?

A
  • fibrous-like and insoluble in H2O

- unaffected by changes in temp and pH

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27
Q

what are examples of fibrous proteins?

A
  • collagen&elastins
  • keratins
  • fibrin
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28
Q

what are collagen and elastin?

A

proteins of CT(tendon and ligament)

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29
Q

what is keratin?

A

protein that is major component of skin and hair

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30
Q

what is fibrin?

A

protein formed when blood clots

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31
Q

what is structure of collagen?

A
  • Glycine every 3rd aa
  • Gly-Pro-Hyp frequent
  • Superhelical cable is formed by H-bonds and Hyp participated
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32
Q

what is hyproxylation?

A

process of putting OH into Prolin to make hyproxyprolin

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33
Q

what is Prolylhydroxylae?

A

required for Hyp formation

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34
Q

what are effect of Scurvy?

A

bleeding gums, loss of teeth, periodontal disease

35
Q

what are characteristics of globular proteins?

A
  • interior nonpolar residues
  • polar, charged on surface
  • regulatory, maintenance and catalytic roles
  • either dissolve or form colloidal suspensions in water
  • sensitive to temp and pH change
36
Q

what are EX of globular proteins?

A

hormones, antibodies, and enzymes

37
Q

what are characteristics of enzymes?

A
  • mediate energy conversion
  • catalytic power and specificity
  • proteins that have single polypeptide, multiple subunits, multienzyme complex
  • sometimes is RNA
38
Q

biological catalytic features of enzymes

A

-dont change equilibrium, not consumed; present at low []; reactants are present at low []; function in mild condition of temp, pH, and pressure; RXN would not normally proceed w/o enzymes;accelerate RXN rates 106to1012; activity depends on structural integrity; high degree of specificity; activity can be precisely regulated

39
Q

Are enzymes regulatory elements?

A

yes

40
Q

How can enzyme control rates of physiological processes?

A
  • by amount of enzymes available
  • enzymatic activity- allosteric control(modulation of activity by changes in [S], activators and inhibitors), isozymes or multiple forms of enzyme, covalent modifications
41
Q

what is isozyme?

A
  • different forms that catalize same RXN
  • different genes-different aa sequence
  • different kinetics
  • regulated differently
42
Q

what are EX of isozyme?

A

lactate dehydrogenase, heart isoform, muscle isoform

43
Q

how to modify enzymes post-translationally?

A
  • cleavage of peptide bond

- chemical modification

44
Q

cleavage of peptide bond

A
  • irreversible

- activates enzyme from inactive precursor.EX: activation of zymogens

45
Q

chemical modification

A
  • phosphotylation of a hydroxyl-containing residue(Ser,Thr, Tyr)
  • acetylation
  • hydroxylation(Proline, Lysine residues in collagen)
  • glycosylation
  • methylation(Histidine)
46
Q

phosphorylation

A
  • reversible

- bidirectional-can acitvate enzyme by adding phosphate (phosphatase) or inhibit by removing phosphate(kinase`)

47
Q

glycosylation

A
  • attachment of linear and branched carbohydrate chains

- atteched at side chain of Asparagine, Serine, Threonine

48
Q

gama-carboxylation

A

of Glutamate in prothrombin, an essential blood-clotting factor, vitamin K required

49
Q

what is role of carbohydates in living organisms?

A
  • supply biological energy via glycolysis and TCA cycle
  • energy stores, metabolic intermediates (structural components of cell membrane and extracellular matrix)
  • framework for DNA,RNA(ribose, deoxyribose)
  • linked to proteins(mediating activity)
50
Q

what is structure of carbohydrate?

A

polyhydroxylated hydrocarbons up to 7C that have carbonyl groups

51
Q

types of Carb?

A
  • monosaccharide (glucose, galactose, fructose)
  • disaccharide (sucrose, lactose)
  • oligosaccharide(3-6 monosaccharides)
  • polysaccharide(>6monosaccharides)- starch, glycogen, cellulose
52
Q

triose?

A

monosaccharide that has 3C

53
Q

tetrose?

A

monosaccharide that has 4C

54
Q

EX of aldohexoses

A

galactose, mannose, glucose

55
Q

what are characteristics of smallest Carb?

A
  • 3C, C2 is chiral

- has D & L form, naturally occurs in D form

56
Q

what are characteristics of erythrose?

A

-4C, naturally occurs in D isomer cuz configuration around penultimate C same as in glyceraldehyde (not from direction rotates polarized light, not from R/S configuration)

57
Q

How does glucose create anomers?

A
  • hydroxyl group reacts w/ aldehyde or ketone to form ring–> 2 form of glucose
  • C1 is asymmetric C=anomeric C
58
Q

what are characteristics of glucose ring structure?

A
  • C1 is anomeric, ring is an intramolecular hemiacetal
  • 6-member ring is related to ring found in pyran(glucosepyranose)
  • 5-member ring forms furanose sugars
  • straight chain and cyclic structures in equilibrium whcih lies to side of ring structures
59
Q

what are characteristics of fructose ring structure?

A
  • 6C w/ ketone group
  • reducing sugar
  • C2 is anomeric carbon
60
Q

how to test reducing sugar?

A
  • place sugar in either Benedict’s or Fehling’s solution and heated
  • positive result: sugar reduces Cu++ to Cu+ and red precipitate forms
  • negative result: sugar is not interconverted w/a form that contains a free aldehyde group
61
Q

what are characteristics of Maltose?

A
  • 2 glucose
  • linked by alpha-1,4-glycosidic
  • reducing sugar cuz one glucose has a potentially free aldehyde group
62
Q

what are characteristics of sucrose?

A
  • glucose+fructose
  • alpha,beta-1,2- linkage
  • not reducing sugar cuz either glucose or fructose has a potentially free aldehyde
63
Q

what are characteristics of lactose?

A
  • abundant in milk
  • D-galactose+D-glucose=alpha-lactose
  • beta-1,4-linkage
  • reducing sugar
64
Q

what are characteristics of ribose and deoxyribose?

A
  • 5C aldose, component of nucleic acids
  • C1 and C4 are connected by an O brigde to form to form Furanose ring
  • ribose is converted to deoxyribose by removing OH at C2
65
Q

what is polysaccharide?

A

monosaccharides joined together. EX: starch, glycogen, cellulose

66
Q

what is starch?

A
  • polymers of >200 glucoses

- amylases(like ptyalin in saliva) digest starch to form maltose

67
Q

what is glycogen?

A
  • same as amylopectin
  • alpha-1,4 linked chains of glucose, alpha-1,6 branches
  • higher density of branches
  • in tissus, glucose is converted to glycogen for storage in liver and muscle
68
Q

what is cellulose?

A
  • polymer of >3000 glucoses
  • beta-1,4 linkage
  • indigestable
  • structural component of green (plant cell wall)
69
Q

what is glycosaminoglycans (GAG)?

A
  • alternating copolymers of uronic acid and amino sugar derivative(glucosamine or galactosamine)
  • has sulfate groups
  • if attached to proteins called proteoglycans
  • found in CT and teeth
  • cushioning effect in joint
70
Q

lipids

A
  • soluble in fat solvents
  • insoluble in water
  • polar and non-polar
  • energy storage, structural components of membranes, hormones, vitamin, bile salts, cellular messengers
71
Q

fatty acids

A
  • metabolic fuel, building blocks for other lipids
  • long chain hydrocarbons represented by R-COOH
  • can be saturated, monounsaturated, polyunsaturated
  • most have even # C(14-22, 16-18)
72
Q

acylglycerols

A
  • fatty acid storage and transport, metabolic intermediates and regulation
  • ester formed from FA and glycerol
  • glycerol may be exterified to different extents
  • triacylglycerol- most abundant, fat storage, hydrolyzed by lipases
73
Q

phospholipids

A
  • membrane structurem membrane signal transduction, storage of arachidonic acid
  • has glyceride backbone, 2 FA at C1 and C2
  • alcohol component esterified to phosphoric acid group to form phosphodiester
74
Q

aphingolipids

A

membrane structure, surface antigens

75
Q

ketone bodies

A

metabolic fuel

76
Q

phosphoglycerides

A
  • families differ by C1 uusually saturated and C2 unsaturated
  • 50% of membrane lipids are phosphatidyl choline and phosphatidyl ethanolamine
77
Q

steroids

A
  • derivative of perhydrocyclopentanophenanthrene ring system
  • contain a hydroxyl group at C3 and hydrocarbon chain attached to C17
  • cholesterol is most abundant in animal tissue
78
Q

nucleotides

A
  • cell signaling
  • protein synthesis
  • energy generation
79
Q

cell signaling

A
  • cAMP(cyclic adenosine monophosphate)

- cGMP(cyclic guanosine monophosphate)

80
Q

protein synthesis

A
  • DNA(deoxyribosenucleic acid)
  • mRNA(messenger ribonucleic acid)
  • rRNA(ribosomal ribonucleic acid)
  • tRNA(transfer ribonucleic acid)
81
Q

energy generation

A
  • GDP,GTP(guanosine di, triphosphate)

- ADP, ATP(adenosine di, triphosphate)

82
Q

nucleic acids

A
  • consists of 4 kinds of bases linked to sugar phosphate backbone
  • joined by phosphodiester bond
83
Q

purine

A

adenine, guanine

84
Q

pyrimidine

A

cytosine, thymine, uracil