Biochem Flashcards

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1
Q

Peptide hormones and cell membrane

A

Cannot cross easily, need G protein coupled receptor

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2
Q

Steroid hormones and cell membrane

A

Pass easily

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3
Q

Steroid hormone base structure

A

Three 6 member rings and one 5 membered ring

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4
Q

Dietary lipids first absorbed in

A

Enterocytes in colon

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5
Q

Chylomicrons

A

Exogenous packaged lipids from colon

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6
Q

VLDL

A

Endogenous lipids from liver

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7
Q

After VLDL is deposited turns into

A

IDL

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8
Q

Triacylglcerols

A

Storage lipid in humans

3 fatty acids on 3 hydroxyl groups of a glycerol backbone

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9
Q

Sphingolipids

A

Structural lipids

Cell membrane component

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10
Q

Waxes

A

FA esterified onto alcohol

In humans usually protection and waterproofing (earwax)

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11
Q

Prostaglandins

A

Signaling lipids (20 carbons)

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12
Q

Cholesterol identification

A

Hydroxyl group on the steroid core

Is hydrophilic for interaction with cell membrane

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13
Q

Deamination of cytosine produces

A

Uracil

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14
Q

Retention factor (Rf)

A

Distance traveled by compound
_________________________________
Distance traveled by solvent

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15
Q

Equilibrium membrane potential

A

NO NET ion movement

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16
Q

Hill coefficient

A

Cooperativity of ligand binding

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17
Q

Hill coefficient n=1

A

No cooperativity

Exponential standard substrate binding

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18
Q

Hill coefficient n>1

A

Positive cooperativity

Sigmoidal shape to binding curve

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19
Q

As core electrons increase, ionization energy for valence e- ____________

A

Decreases

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20
Q

Electromagnetic spectrum

Energy of photon is directly proportionate to

A

Frequency

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21
Q

Electromagnetic spectrum

Energy of photon is inversely proportional to

A

Wavelength

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22
Q

Electromagnetic spectrum

As wavelength increases, frequency and energy

A

Decrease

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23
Q

B- decay

A

Neutron converts to proton

Emits electron

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24
Q

B+ decay

A
Proton converts to neutron 
Ejects positron (w/ pos charge)
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25
Q

As atomic number changes

A

Identity of element changes

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26
Q

Does mass number change in beta decay

A

NO BIH

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27
Q

Does mass number change for beta decay

A

No

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28
Q

Peptide bond reaction

A

Nucleophilic substitution rxn

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29
Q

Most abundant protein in eukaryotic cell

A

Actin

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30
Q

Actin size

A

Thin

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31
Q

Myosin size

A

Thick

32
Q

Treadmilling

A

Pos and Neg of actin regulated by ATP

33
Q

New actin monomers add on ______ end

A

Positive

34
Q

Actin monomers dissociate from —— end

A

Negative

35
Q

When atp is bound, actin will

A

Associate

36
Q

Actin myosin crossbridge cycle

A
Ca dump
Ca binds to troponin
Troponin moves tropomyosin out of way
Adp and p
Releases p to bind to myosin binding site
Movement releases adp 
Atp rebinds
37
Q

Mircotubules are important in

A

Structure

Mitosis and meiosis

38
Q

Alpha tubulin location

A

Center of centrosome, interior of cell

39
Q

Beta tubulin location

A

Edges of cell membrane

40
Q

Collagen

A

Helical fiber , ext4acellular CT

BONES TISSUES LIGAMENTS TENDONS

41
Q

Elastin

A

Long and coiled becomes linear with stretch

42
Q

Keratin

A

Epithelial cell protein hair and nails

43
Q

Kinesins

A

Travel to positive end (beta) edge of cell

44
Q

Microtubules made

A

Kinesin and dynein

45
Q

Microtubules are

A

Highways for motor protein

46
Q

Dyneins

A

Travel to negative (alpha) interior of cell

47
Q

Active transport with other molecules

A

Symporter

48
Q

Active transport opposite other molecules

A

Antiporter

49
Q

Signaling proteins

A

Peptide hormones

Antibodies

50
Q

Peptide hormones

A
51
Q

Melting occurs when

A

Enough energy is gained to overcome noncovalent INTERmolecular forces

52
Q

Hydroxide [] is 10-6 what is pH

A

8

53
Q

Formal charge

A

Group valence - non bonding electrons - 1/2 bonding electrons

54
Q

Reducing sugars

A

All monosaccharides

55
Q

Tollens test

A

Silver precipitate

Detects reducing sugars

56
Q

Small protein SDS PAGE

A

Migrate fastest

57
Q

Small proteins size exclusion chromatography

A

Move slower. Get tied up in pores

58
Q

Large proteins size exclusion chromatography

A

Move fastest

59
Q

Reducing agents in SDS page and size exclusion chromatography

A

Reduce disulfide bonds

60
Q

SDS page and SEC with reducing agent

A

Proteins run at monomeric size

61
Q

D amino acids

A

UNCOMMON IN NATURE

62
Q

Amino acid form most common in nature

A

L amino acids

63
Q

Enantiomers

A

Share same physical and chemical properties

Differ at all chiral centers

64
Q

In dipeptide n terminus is on

A

LEFT

65
Q

In dipeptide C terminus is on

A

RIGHT

66
Q

Mitochondrial gene therapy

A

Targets mitochondrial dna only, not nuclear dna

67
Q

B oxidation occurs in

A

Mitochondria

68
Q

Disulfide bonds unlikely to form in

A

Cytosol

69
Q

Disulfide bonds likely to form in

A

Endoplasmic reticulum

70
Q

Sp3

A

Tetrahedral

71
Q

Octahedral has

A

No lone pairs

72
Q

Square planar has

A

Two lone pairs

73
Q

Dsp3 with one lone pair

A

See saw

74
Q

Dsp3 with two lone pairs

A

T shaped geometry

75
Q

Lewis base

A

Electron pIr donor

76
Q

Lewis acid

A

Electron pair acceptor

77
Q

Bros Ted Lowry and Arrhenius

A

Must move hydrogens