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Biological Sciences Flashcards

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1
Q

Fats are broken down to two components that are used in cellular respiration:

A

glycerol and fatty acids

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2
Q

How/where does glycerol enter the cellular respiration pathway?

A

glycerol is converted to one of the intermediate products of glycolysis

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3
Q

How/where do fatty acids enter the cellular respiration pathway?

A

fatty acids are converted through beta-oxidation to acetyl coA and enter the Krebs cycle

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4
Q

Myosin:

A

motor protein that moves along microfilament “tracks”

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5
Q

Phospholipids:

A

non-polar tail region and polar phosphate head

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6
Q

Cholesterol:

A

amphipathic molecule; maintains membrane rigidity at higher temperatures, fluidity at lower temperatures

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7
Q

Nervous tissues:

A

neurons, glial cells

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8
Q

Glial cells:

A

supporting cells of the nervous system (non-neurons): astrocytes, microglia, Schwann cells, oligodendrocytes, ependymal cells

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9
Q

Ependymal cells:

A

found on the lining of the ventricles of the brain as well as the spinal cord’s central canal; could be classified as nervous or epithelial tissues

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10
Q

Connective tissues:

A

include bone, cartilage, lymphatic tissue, fat (adipose tissue), tendons, and ligaments

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11
Q

Muscle tissues:

A

any skeletal, smooth, or cardiac muscle cells

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12
Q

Smooth muscle tissues fuction:

A

responsible for contractility of hollow organs, such as blood vessels or the bladder

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13
Q

Paracrine communication:

A

local; signal molecules secreted by one cell bind to receptors on another

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14
Q

Autocrine communication:

A

signal molecules secreted by a cell bind to receptors on that same cell

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15
Q

Intacrine communication:

A

signal molecules (usually steroids) bind to receptors inside the same cells that produced them, without ever being secreted outside the cell

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16
Q

Juxtacrine communication:

A

signaling required direct contact between two cells

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17
Q

Glucose/fructose chemical formula:

A

C6H12O6

(glucose - aldehyde, fructose - ketone)

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18
Q

Glucose polysaccharides:

A

glycogen, starch, cellulose

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19
Q

Glycogen:

A

branched, alpha-linked glucose polymer, used for storage in animals

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20
Q

Starch:

A

branched, alpha-linked glucose polymer, used for storage in plants

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21
Q

Cellulose:

A

beta-linke glucose polymer, used for storage in plants, indigestible in animals without help from symbiotic bacteria

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22
Q

2 important characteristics of peptide bonds:

A
  1. lack of rotation around the bond
  2. electron density is spread out between N, C, and O of the amide (resonance)
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23
Q

1) Ending -ase means…
2) Ending *-tase *means…

A

1) Enzyme
2) ATP-requiring enzyme

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24
Q

6 interactions responsible for tertiary protein structure:

A

1) hydrogen bonding
2) disulfide bonds
3) hydrophobic/hydrophilic interactions
4) ionic interactions
5) Van der Walls forces
6) proline turns

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25
Q

5 kinds of lipids:

A

1) fatty acids
2) triacylglycerols
3) phospholipids
4) steroids
5) glycolipids

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26
Q

Amphipathic lipids:

A

fatty acids, phospholipids, glycolipids

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27
Q

3 components of a nucleotide:

A

sugar backbone, nitrogenous base, phosphate group

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28
Q

What are some common nucleotides?

A

DNA, RNA, cAMP, NADH, FADH2, FMN, Coenzyme A, ATP, GTP, UTP

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29
Q

Order of metabolism:

A

healthy individuals burn carbohydrates first, then fats, then proteins

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30
Q

Amino acid order of deprotonation:

A

1) carboxylic acid hydrogen
2) any acidic hydrogen on R-group
3) amine group hydrogen

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31
Q

Lac operon - glucose present:

A

Low levels of cAMP, CAP inactive, doesn’t bind to DNA, RNA polymerase doesn’t bind to promoter

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32
Q

Lac operon - lactose present:

A

binds to inhibitor, inhibitor cannot bind to operator site, RNA polymerase can bind to promoter

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33
Q

Lac operon - 3 upstream sites in order:

A

CAP, promoter, operator

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34
Q

DNA polymerase reads the template strand in the __ to __ direction:

A

3’, 5’

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35
Q

During translation, mRNA is read (by ribosomes) in the __ to __ direction.

A

5’, 3’

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36
Q

Missense mutation (DNA):

A

a mutation that changes the codon such that a different amino acid will be incorporated

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37
Q

Silent mutation (DNA):

A

any mutation that does NOT alter the amino acid sequence

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38
Q

Frameshift mutation (DNA):

A

any mutation that changes the reading frame

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39
Q

Nonsense mutation (DNA):

A

a mutation that changes a normal codon into a premature stop codon

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40
Q

P1 generation (genetics):

A

first homozygous parental generation

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41
Q

F1 generation (genetics):

A

offspring from P1; heterozygous

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42
Q

F2 generation (genetics):

A

offspring of F1 generation; 3:1 phenotypic ratio (Mendelian ratio) and 1:2:1 genotypic ratio

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43
Q

Incomplete dominance (genetics):

A

ex: RR gives red flowers, rr gives white flowers, Rr gives pink flowers

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44
Q

Co-dominance (genetics):

A

ex: RR gives red flowers, rr gives white flowers, Rr gives red and white striped flowers

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45
Q

Incomplete penetrance (genetics):

A

various individuals all have identical genotypes and yet some get the disease phenotype and others do not

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46
Q

Limited expressivity (genetics):

A

various individuals all have the same genotype AND all of them have the disease phenotype (i.e., 100% penetrance), but individuals are impacted in varying degrees

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47
Q

Polygenic (genetics):

A

many genes contribute toward one phenotypic trait

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48
Q

Pleiotropy (genetics):

A

one single gene contributes to multiple phenotypic traits

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49
Q

Mosaicism (genetics):

A

different cells within the same individual contain non-identical genotypes

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50
Q

Genetic imprinting:

A

one specific gene is expressed differently depending on which parent it originated from

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51
Q

Epigenetic:

A

any heritable phenotype resulting from any process other than a change in the DNA sequence itself (ex: factors affecting gene expression)

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52
Q

Linkage (genetics):

A

two genes are close enough to each other on the same chromosome that it is unlikely a crossing over event will occur exactly between them

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53
Q

Polymorphisms:

A

random variations in genetic sequence among individuals that create variable forms; usually due to mutation, and may or may not be increasingly represented in future generations depending on whether or not that particular variation in form provides an evolutionary fitness advantage

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54
Q

Speciation:

A

the formation of new species from existing ones

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55
Q

Adaptive radiation (genetics):

A

the rapid formation of a variety of species from one ancestral species—usually characterized by a strong environment-species connection (ex: one species of turtle migrated to five different environments and rapidly formed five different species based on natural selection driven by the unique characteristics of each environment)

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56
Q

Evolutionary bottleneck:

A

sudden decrease in the number of individuals in a population

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57
Q

Genetic drift:

A

a change in the allele frequency within a population due to random, non-genetic, non-selective factors (ex: meteorite striking the earth)

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58
Q

Carrying capacity:

A

maximum number of individuals an ecosystem or environment can sustain

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59
Q

Hardy-Weinberg formulas:

A

p + q = 1

p2 + 2pq + q2 = 1

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60
Q

What do p and q represent (Hardy-Weinberg)?

A

the fractions of p and q alleles in the population

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61
Q

What do p2, q2 and 2pg represent (Hardy-Weinberg)?

A

fractions of individuals with each possible genotype

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62
Q

What does p2 represent (Hardy-Weinberg)?

A

the fraction of individuals who have the homozygous dominant genotype

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63
Q

What does q2 represent (Hardy-Weinberg)?

A

the fraction of individuals with the homozygous recessive genotype

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64
Q

What does 2pg represent (Hardy-Weinberg)?

A

the fraction of individuals with the heterozygous genotype

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65
Q

Taxonomical classification levels:

A

kingdom, phylum, class, order, family, genus, species (mnemonic: King Phillip cried out for good soup)

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66
Q

Human taxonomy:

A

Animalia, Chordata, Mammalia, Primates, Hominidae, Homo, (Homo) sapiens (mnemonic: All cool men prefer healthy hot sex)

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67
Q

Heterotrophs:

A

cannot fix CO2 and therefore must ingest organic molecules such as carbohydrates as their carbon source

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68
Q

Chemotrophs:

A

oxidize organic or inorganic compounds to harvest energy

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69
Q

Phototrophs:

A

can capture their own energy directly from the sun via photosynthesis

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70
Q

Autotrophs:

A

capable of fixing CO2 and can therefore use CO2 as their carbon source for synthesizing organic molecules

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71
Q

Viruses:

A

viruses are acellular and cannot survive, grow or reproduce on their own; they require a host to accomplish most if not all of the functions we normally associate with “living things”

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72
Q

Major components of all viruses:

A

nucleic acid (DNA or RNA but never both) and proteins

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73
Q

Enveloped viruses structure:

A

small circular membranes surrounding a protein capsid and the nucleic acid

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74
Q

Retrovirus:

A

contains a specific enzyme called reverse transcriptase that can translate its RNA nucleotide sequence into DNA (because RNA could not be incorporated into the host’s genome)

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75
Q

Bacterial transformation:

A

a bacteria picks up DNA from the environment and incorporates it into its own DNA

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76
Q

Bacterial transduction:

A

viruses accidentally incorporate host genetic material into their nucleic acids

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77
Q

Gram postive bacteria (purple):

A

thick cell wall, single cell membrane, form endospores

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78
Q

Gram negative bacteria (pink):

A

thin cell wall, two cell membranes (one inside the cell wall, one outside), do not form endospores

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79
Q

Endospore:

A

dormant, tough, and non-reproductive structure produced by certain bacteria

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80
Q

sp hybridized shape:

A

linear

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81
Q

sp2 hybridized shape:

A

trigonal planar, bent

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82
Q

sp3 hybridized shape:

A

tetrahedral, trigonal pyramidal

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83
Q

Boron and beryllium are stable with only __ electrons in their valence shells.

A

6

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84
Q

Formal charge =

A

of valence electrons - (non-bonded electrons + # of bonds)

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85
Q

Ester functional group:

A

O

||

R – C – OR

(-oate ending, H-bond recipients but not donors)

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86
Q

Amine functional group:

A

R – NH2

(act as bases or nucleophiles, basicity decreases from tertiary-primary, capable of hydrogen bonding)

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87
Q

Amide functional group:

A

O

||

R -- C -- NR<sub>2</sub>

(carbonyl carbons unreactive, can hydrogen bond, resonance limits rotation)

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88
Q

Anhydride functional group:

A

O O

|| ||

R – C – O – C – R

(the 2 carbonyl carbons are highly reactive because leaving group is resonance-stabilized carboxylate ion)

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89
Q

Aryl functional group:

A

aromatic ring – R

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90
Q

Hydrazide functional group:

A

NH2 – NH – R

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91
Q

Nitrile functional group:

A

R – C = N

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92
Q

Imine functional group:

A

N – R

||

R – C – R

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93
Q

Enamine functional group:

A

C = C – N

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94
Q

Sulphone functional group:

A

O = S = O

/ \

R R

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95
Q

Acetal functional group:

A

two ethers on same carbon

RO – CH – OR

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96
Q

Ketal functional group:

A

two ethers on same carbon

RO – C – OR

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97
Q

Hemiacetal functional group:

A

RO

|

 R -- CH -- OH
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98
Q

Hemiketal functional group:

A

RO – C – OH

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99
Q

Optically active (O-chem):

A

a substance does rotate plane-polarized light

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100
Q

Racemic mixture (O-chem):

A

a 50/50 mix of the two absolute configurations of a compound (R and S)

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101
Q

Epimers:

A

diastereomers that differ at only one chiral center

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102
Q

Anomers:

A

molecules that differ only in their spatial orientation at the anomeric carbon (bonded to the 2 oxygens) of a ring structure

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103
Q

Decarboxylation:

A

R-carboxylic acid → R + CO2

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104
Q

IR absorbance - carbonyl C=O:

A

1700 cm-1; sharp, deep

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105
Q

IR absorbance - alcohol, OH:

A

3300 cm-1; broad, separate from CH

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106
Q

IR absorbance - saturate alkane, CH:

A

2800 cm-1; sharp, deep

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107
Q

IR absorbance - carboxylic acid, OH:

A

3000 cm-1; broad, overlaps CH

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108
Q

IR absorbance - amine, NH:

A

3300 cm-1; broad, shallow

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109
Q

IR absorbance - amide, NH:

A

3300 cm-1; broad, deep

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110
Q

IR absorbance - nitriles, C_=_N:

A

2250 cm-1; sharp, deep

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111
Q

Sec-butyl:

A

– CHCH2CH3

|

CH<sub>3</sub>
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112
Q

Isobutyl:

A

– CH2CHCH3

|

 CH<sub>3</sub>
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113
Q

Tert-butyl:

A

CH3

|

    -- C -- CH<sub>3</sub>

|

  CH<sub>3</sub>
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114
Q

IR spectroscopy:

A

when vibrational frequencies of dipolar bonds match the frequency of IR radiation, the bond will absorb some of the IR energy

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115
Q

IR spectroscopy - The vibrational frequency of a dipolar bond is determined by:

A
  1. strength of the bond (weaker = lower frequency)
  2. molecular weight of the atoms involved in the bond (larger atom = lower frequency)
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116
Q

UV spectroscopy:

A

electrons within a molecule absorb the energy of electromagnetic radiation and “excite” to a higher energy level

  • only single bonds = low or no absorbance
  • increasing absorbance: double < triple < conjugated bonds
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117
Q

Mass spectrometry:

A

molecule bombarded with electrons and fragmented, accelerated through a narrow curved magnet, strength of magnetic field increased until all fragments follow curved path into a detector

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118
Q

NMR spectroscopy:

A

an atom must have either an odd atomic number or an odd mass number to register on an NMR

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119
Q

What is Rf? (thin-layer chromatography)

A

distance traveled by component / distance traveled by solvent

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120
Q

A __ abstracts a proton and a __ attacks a carbon.

A

base, nucleophile

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121
Q

E1 reaction:

A
  1. leaving group dissociates, forming carbocation (slow step)
  2. proton abstracted, double bond formed (fast step)
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122
Q

E2 reaction:

A
  1. proton abstracted, double bond forms, leaving group ejected
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123
Q

An E_ reaction requires a strong base, while an E_ does not.

A

2, 1

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124
Q

Sn1 reaction:

A
  1. leaving group dissociates, carbocation formed (slow step)
  2. attack of carbocation by nucleophile (fast step)
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125
Q

Sn2 reaction:

A
  1. “back-side attack” of the electrophile, leaving group simultaneously ejected
126
Q

Which halides react with alkanes in radical halogenation?

A

fluorine, chlorine, bromine

127
Q

Halogen reactivity:

A

F > Cl > Br

(bond mostly to least-substitued carbon)

128
Q

Halogen selectivity:

A

Br > Cl > F

(bond mostly to most-substitued carbon)

129
Q

Hydrogenation (addition reaction):

A

C=C + H2+ metal catalyst = CH3CH3

(syn reaction)

130
Q

Hydrogen bond acceptors:

A

N, O or F with at least one lone pair of electrons

131
Q

Hydrogen bond donors:

A

H connected to a highly electronegative atom, such as N, O or F

132
Q

Zaitsev’s rule:

A

the major product of an elimination reaction is the more substituted alkene

133
Q

Alcohol acidity:

A
  1. alcohols are less acidic than water
  2. alcohol acidity increases from tertiary to secondary to primary
134
Q

SN2 formation of alkyl halide from an alcohol:

A

(for UN, 1o or 2o alcohols)

  1. CH3OH + HX → CH3OH2+ + X-
  2. X- attacks central carbon, water molecule ejected
135
Q

SN1 formation of alkyl halide from an alcohol:

A

(for 3o alcohols)

  1. R3OH + HX → CH3OH2+ + X-
  2. water dissociates, carbocation formation (rate limiting step)
  3. X- attacks the carbocation
136
Q

Oxidation of alcohol:

A

1o alcohols → aldehydes → carboxylic acids

2o alcohols → ketones

3o alcohols → cannot be oxidized

137
Q

Pinacol rearrangement:

A

vic-diol + hot acid → ketone (tetra-sub) or aldehyde (tri-sub)

138
Q

Protection of alcohols:

A

protect alcohols from oxidation while still allowing reaction to occur with other functional groups on molecule (O-H → O-protection + H+ → O-H)

139
Q

Inorganic substitutions:

A

ROH + SOCl2 or PBr3 → RCl or RBr

140
Q

Formation of tosylates/mesylates:

A

Tosyl/Mesyl-Cl + ROH → Tosyl/Mesyl-OR + HCl

(SN2 reaction)

141
Q

Acid-catalyzed dehydration (elimination reaction):

A
  1. protonation of alcohol
  2. ‘leaving group’ leaves, forming carbocation (E1 only)
  3. water molecules takes a proton, electrons collapse to form double bond (ejecting leaving group in E2)
142
Q

Grignard Synthesis:

A
  • produces an alcohol by adding RMgX to a carbonyl
  • R acts as carbanion, attacks electrophilic carbonyl carbon, breaks double bond, negatively charged O is protonated to form alcohol
143
Q

Ether properties:

A

very non-reactive, weakly polar, low boiling points, excellent solvents

144
Q

Substitution of an epoxide:

A

forms alcohol - severe ring strain, reaction can proceed via SN1 or SN2

145
Q

Excretory system functions:

A
  • excrete liquid and solute wastes, e.g., water, excess salts, nitrogenous waste
  • maintain pH, osmolarity, blood pressure
146
Q

Osmolarity:

A

number of osmoles of solute per liter

147
Q

Osmole:

A

the amount of solute that dissociates in solution to form one mole of particles (molecules and ions)

148
Q

Net effect of aldosterone on kidney function:

A

water retention and increased blood pressure

149
Q

Net effect of ADH on kidney function:

A

water retention and increased blood pressure

150
Q

Respiratory system functions:

A

gas exchange at alveoli - chemiosmosis of oxygen to blood, CO2 out of blood back into lungs

151
Q

Inhalation - path of air:

A

mouth/nose → pharynx → larynx → trachea → bronchi → bronchioles → alveoli

152
Q

The diaphragm moves __ when it is flexed and __ when it is relaxed.

A

down, up

153
Q

The diaphragm moves down during __ and up during __.

A

inhalation, exhalation

154
Q

Hemoglobin:

A

protein made of four protein chains, each with one heme, each heme holding one O2 molecule

155
Q

How CO2 is carried in the blood:

A

CO2 + H2O → HCO3- + H+

156
Q

Functions of the cardiovascular system:

A
  • deliver oxygen and nutrients to the cells and tissues of the body
  • pick up CO2 and waste products and deliver them to lungs and kidneys
157
Q

Arteries __ the heart, veins __ the heart.

A

leave, return to

158
Q

Systemic circulation:

A

blood flows from the left ventricle, through the arteries, arterioles, capillaries, venules, veins, vena cava and back to the right atrium

159
Q

Pulmonary circulation:

A

blood flows from the right ventricle, through the pulmonary arteries to the lungs and back through the pulmonary veins to the left atrium

160
Q

Blood vessels:

A

arteries → arterioles → capillaries → venules → veins

161
Q

Erythrocytes:

A

(red blood cells) essentially membrane-bound sacks of hemoglobin, mature RBCs have no nucleus or other organelles

162
Q

Leukocytes:

A

(white blood cells) no hemoglobin, normal cells with all their organelles

163
Q

Granulocytes:

A

these cells live for hours to days

164
Q

Agranulocytes:

A

these cells live for months to years

165
Q

Hematopoiesis:

A

development of all blood cells from stem cells in the bone marrow

166
Q

Platelets:

A

tiny, membrane-bound drops of cytoplasm

167
Q

Antigens:

A

any substance that causes your immune system to produce antibodies against it

168
Q

Four blood types:

A

A, B, AB, O

169
Q

Antigens present on blood cell membranes:

A

Type A - A antigens only

Type B - B antigens only

Type AB - Both A and B antigens

Type O - neither A nor B antigens

170
Q

Universal blood donor:

A

Type O (no antigens)

171
Q

Universal blood recipient:

A

Type AB (donor antigens will be A, B or none)

172
Q

Function of lymphatic system:

A
  • gather excess interstitial fluid and return it to blood
  • remove from interstitial spaces proteins and other molecules too big to be taken up by the capillaries
  • monitor the blood and lymph for infection
173
Q

Lymph nodes are filled with __.

A

lymphocytes

174
Q

Two main lymphatic vessels:

A
  1. right lymphatic duct
  2. thoracic duct

(both merge with large veins in lower portion of neck)

175
Q

The nervous system includes:

A

brain, spinal cord, peripheral nerves, neural support cells, sensory organs such as eyes and ears

176
Q

Neurons depends entirely on __ for energy.

A

glucose

177
Q

Neurons have very low __ and thus require high __.

A

glycogen & oxygen storage capability, blood flow

178
Q

Perfusion:

A

blood flow

179
Q

Neural impulses can only flow in one direction:

A

cell body to synapse

180
Q

T/F - The action potential that arrives at the terminal button is the same stimulus that begins at the dendrites.

A

False

181
Q

Resting potential value:

A

-70 mV

182
Q

Action potential:

A

a dramatic change in the resting electrical potential across the membrane of a nerve cell

183
Q

Sodium/potassium pump:

A

3 Na+ ions out, 2 K+ ions in; net effect is more positive charge outside, more negative charge inside

184
Q

Voltage-gated sodium channels:

A

integral proteins that change shape when resting potential disturbed; when ‘open,’ Na+ rushes back into cell

185
Q

Depolarization:

A

spike in membrane potential when voltage-gated channels opened, from -70 mV to approx +40 mV

186
Q

Threshold potential (to trigger full action potential):

A

-55 mV

187
Q

Voltage-gated potassium channels:

A

react to (almost) maximum depolarization, open and begin to send K+ ions back outside the cell

188
Q

Repolarization:

A

open potassium channels decreases membrane potential from 40 mV back to -70 mV

189
Q

Hyperpolarization:

A

membrane potential temporarily dips to approx -90 mV as resting potential is restored

190
Q

Absolute refractory period:

A

a second stimulus cannot initiate a response in the neuron until the membrane is repolarized

191
Q

Effector (CNS):

A

the membrane of a muscle or other target (not another neuron) of a neurotransmitter

192
Q

Voltage-gated calcium channels:

A

when action potential arrives at presynaptic membrane, channels triggered to allow calcium flow into cell - Ca+ ion increases triggers activity of neurotransmitter bundles

193
Q

Acetylcholinesterase:

A

enzyme in the synaptic cleft that breaks down neurotransmitters (stopping the signal)

194
Q

Afferent neurons:

A

sensory neurons

195
Q

Efferent neurons:

A

motor neurons

196
Q

Interneurons:

A

connect afferent and efferent neurons (the brain and 90% of all other neurons are interneurons)

197
Q

Sympathetic:

A

“fight or flight”

198
Q

Parasympathetic:

A

“rest and digest”

199
Q

Somatic nervous cells:

A

voluntary, innervate skeletal muscle

200
Q

Autonomic nervous cells:

A

involuntary, innervate cardiac muscle, smooth muscle and glands

201
Q

Sympathetic neurotransmitter:

A

acetylcholine at the ganglia, norepinephrine at the effector

202
Q

Parasympathetic neurotransmitter:

A

acetylcholine

203
Q

Rods:

A

highly sensitive, perceive black & white only

204
Q

Cones:

A

less sensitive than rods, perceive color

205
Q

The ciliary muscles __ to __ the curvature of the lens.

A

contract, increase

206
Q

Outer ear:

A

pinna (earlobe), auditory canal

207
Q

Middle ear:

A

tympanic membrane (eardrum), 3 middle ear bones: malleu, incus & stapes

208
Q

Inner ear:

A

cochlea, semicircular canals, vestibulocochlear nerve

209
Q

Exocrine glands:

A

release enzymes and other liquids into the body’s external environment

210
Q

Endocrine glands:

A

release hormones into the internal fluids of the body (blood, lymph, etc.)

211
Q

All steroids are __ derivatives.

A

cholesterol

212
Q

Transport: Lipid-soluble hormones require:

A

a protein carrier or micelle/vesicle

213
Q

Transport: Peptide hormones:

A

water-soluble, readily dissolve in blood

214
Q

Target: Lipid-soluble hormones act almost exclusively:

A

on or inside the nucleus

215
Q

Target: Peptide hormones:

A

act on a variety of cell locations

216
Q

T/F - Lipid-soluble hormones require a cell membrane receptor.

A

false

217
Q

Function of hormones:

A

return the body to homeostatic (“normal”) conditions

218
Q

The ability to “fix” carbon is…

A

the ability to capture CO2 and integrate that carbon into larger macromolecules

219
Q

Digestive system function:

A

physical digestion - separate food molecules from each other

chemical digestion - break molecules into their monomers for absorption

220
Q

Chemical digestion in the mouth acts on __ only via the enzyme __.

A

carbohydrates, amylase

221
Q

Epiglottis:

A

“closes” when swallowing, allowing food/liquid down esophagus only

222
Q

The __ is the first site of protein digestion:

A

stomach

223
Q

The enzyme __ catalyzes hydrolysis of proteins.

A

pepsin

224
Q

Functions of the liver:

A
  • produces bile (stored and concentrated in gall bladder)
  • Filters blood
  • Produces blood plasma proteins
  • Produces cholesterol (LDL, HDL, etc.)
225
Q

Glycogenolysis:

A

breakdown of glycogen stored in liver to form free glucose for release in blood (stimulated by glucagon)

226
Q

Glycogenesis:

A

synthesis in the liver of glycogen for storage (stimulated by insulin)

227
Q

Pancreas functions:

A

secretes digestive enzymes and hormones

228
Q

Gallbladder function:

A

stores and concentrates bile, but does not produce bile

229
Q

Function of bile:

A

emulsifies fats (physical digestion) in small intestine

230
Q

Small intestine function:

A

majority of all digestion and absorption

231
Q

Large intestine function:

A

water & vitamin absorption

232
Q

Villi:

A

finger-like projection on wall of small intestine (increase surface area available for absorption)

233
Q

Carbohydrate digestion:

A

begins in mouth, broken down to monomers before absorption, enter the blood stream and travel to liver

234
Q

Protein digestion:

A

begins in stomach, broken down to small peptides and amino acids before absorption, enter bloodstream and travel to liver

235
Q

Lipid digestion:

A

begins in small intestine, enter the lacteals

236
Q

Immune system function:

A

protect body from infection and disease, destroy pathogens invading the body

237
Q

Function of spleen:

A

filters blood, storage of high amount of blood to combat hemorrhagic shock, breaks down and recycles old RBCs

238
Q

Duodenum:

A

upper portion of the small intestine

239
Q

Cell-mediated immunity:

A

self-attack of diseased cells, involves T-lymphocytes

240
Q

Humoral immunity:

A

antibodies and primary/secondary response, involve B-lymphocytes

241
Q

Function of integumentary system:

A

protect against abrasion, physical barrier to pathogens, temperature regulation, vitamin D synthesis, prevention of water loss

242
Q

Sarcomere:

A

repeating units of interconnected actin and myosin fibers

243
Q

Sarcomere - A band:

A

length of the myosin filament

244
Q

Sarcomere - I band:

A

distance between ends of myosin filaments

245
Q

Sarcomere - H zone:

A

distance between ends of actin filaments

246
Q

Sarcomere - Z line:

A

defines the edge of each individual sarcomere unit

247
Q

Sarcomere - M line:

A

the very center of the myosin filament

248
Q

The only neurotransmitters used at neuromuscular junctions is __.

A

acetylcholine

249
Q

Muscle contraction - role of ATP:

A

binds to myosin head after “power stroke” facilitating its release from actin filament

250
Q

Muscle contraction - role of Ca+:

A

move tropomyosin out of the way, allow myosin to bind to actin

251
Q

Features of skeletal muscles:

A

store large amounts of glycogen, require lots of oxygen (use myoglobin)

252
Q

Joint types:

A
  • fibrous (skull bones)
  • cartilaginous (ribs to sternum)
  • synovial (knee, elbow, etc.)
253
Q

Cartilage:

A

a connective tissue composed mostly of collagen

254
Q

Acrosome:

A

structure on the tip of the head of each sperm, contains digestive enzymes to dissolve otherwise impenetrable coating of ovum

255
Q

Ovulation requires a __ in hormone levels; menstruation requires a __.

A

surge, decline

256
Q

3 germ layers:

A

ectoderm, mesoderm, endoderm

257
Q

The carbonyl double bond is __ than an alkene.

A

shorter and stronger

258
Q

Carbonyl alpha hydrogens are:

A

acidic (the greater the partial positive charge on the carbonyl carbon, the more acidic)

259
Q

Formaldehyde:

A

HCOH

260
Q

Acetaldehyde:

A

CH3COH

261
Q

Benzaldehyde:

A

C6H5COH

262
Q

Acetone:

A

CH3COCH3

263
Q

Aldehydes and ketones can act as H-bond __ but not as H-bond __.

A

recipients, donors

264
Q

Aldehydes and ketones undergo __.

A

nucleophilic addition

265
Q

Carboxylic acids/esters/amides/anhydrides undergo __.

A

nucleophilic substitution

266
Q

Halogenation of aldehyde/ketone:

A

substitution of a Br, Cl or I for one of the alpha hydrogens on an aldehyde/ketone

267
Q

Haloform reaction:

A

halogenation of a methyl ketone with sufficient halogen present to replace all three alpha hydrogens

268
Q

Aldol condensation:

A

the condensation of one aldehyde or ketone with another aldehyde or ketone

(alpha hydrogen abstracted by a base, carbanion forms, attacks carbonyl carbon, oxygen protonated to form an alcohol)

269
Q

alpha-beta unsaturated carbonyls:

A

aldehydes or ketones with a double bond between the alpha and beta carbons

270
Q

Hofmann degradation:

A

primary amides (-NH2) react with Cl2 or Br2 to form primary amines + CO2

271
Q

Wittig reaction:

A

carbonyl → alkene

272
Q

Formic acid:

A

HCOOH

273
Q

Acetic acid

A

CH3COOH

274
Q

Benzoic acid

A

C6H5COOH

275
Q

Carboxylic acid hydrogen bonding:

A

can do it twice to form dimers

276
Q

Decarboxylation:

A

R-carboxylic acid → R + CO2

277
Q

Esterification:

A

carboxylic acid + alcohol → ester + H2O

278
Q

Formation of acid chlorides:

A

carboxylic acid + PCl3 → RCOCl + H2O

(very reactive because high withdrawing power of chlorine, and chloride ion is excellent leaving group)

279
Q

Electron donating/withdrawing:

A

atoms with full or partial positive charges withdraw; atoms with full or partial negative charges donate

280
Q

Halide leaving groups - best to worst:

A

I → Br→ Cl → F

281
Q

What is peristalsis?

A

the involuntary constriction and relaxation of the muscles of the intestine or another canal, creating wavelike movements that push the contents of the canal forward

282
Q

At low pH, amino acids exist in the __ form.

A

cationic

283
Q

At high pH, amino acids exist in the __ form.

A

anionic

284
Q

What are the three basic amino acids?

A

HAL - histidine, lysine, arginine

(side chains contain an amine group)

285
Q

What are the two acidic amino acids?

A

aspartic acid, glutamic acid

(side chains contain a carboxylic acid)

286
Q

Glycine’s unique feature:

A

R group is hydrogen, making it optically inactive

287
Q

Proline’s unique feature:

A

helix breaker

288
Q

L-amino acids:

A

more common in nature, only type found in proteins

289
Q

Non-polar amino acids:

A

VIP MALT Ph Glycine

(Valine, Isoleucine, Proline, Methionine, Alanine, Leucine, Tryptophan, Phenyalanine, and Glycine)

290
Q

Steroid hormones:

A

PET AC

(progesterone, estrogen, testosterone - gonads; aldesterone, cortisol - adrenal cortex)

291
Q

Anterior pituitary hormones:

A

FLAT PiG

292
Q

FSH function:

A

growth of follicle, production of sperm

293
Q

LH function:

A

surge causes ovulation, stimulates secretion of estrogen & testosterone

294
Q

ACTH function:

A

stimulates adrenal cortex to release stress hormones

295
Q

TSH function:

A

stimulates release of T3 & T4 from thyroid

296
Q

Prolactin function:

A

stimulates millk production in breasts

297
Q

hGH function:

A

stimulates growth throughout the body

298
Q

ADH function:

A

collecting duct of kidney becomes highly water-permeable, concentrating the urine

299
Q

Oxytocin function:

A

stimulates contractions during labor, milk secretion during nursing

300
Q

T3 & T4 functions:

A

increase basal metabolic rate, overall regulation of metabolism

301
Q

Calcitonin function:

A

inhibits osteoclasts, decreases blood calcium

302
Q

Parathyroid hormone function:

A

increases blood calcium - stimulates osteoclasts, uptake of Ca2+ in gut, reabsorption of Ca2+ in kidney

303
Q

Epinephrine/norepinephrine functions:

A

response almost identical to “fight or flight”

304
Q

Aldesterone function:

A

regulation of blood pressure - increased water and Na+ retention, K+ secretion

305
Q

Cortisol function:

A

stress hormone - increase blood sugar through gluceogenesis, aid carb/fat/protein metabolism

306
Q

Progesterone function:

A

growth and maintenance of uterus during pregnancy

307
Q

Estrogen function:

A

stimulates female sex organs, causes LH surge in menstruation

308
Q

Testosterone function:

A

development of secondary sex characteristics

309
Q

hCG function:

A

maintenance of corpeus luteum during pregnancy

310
Q

Aldehyde ending:

A

-al

311
Q

Enols:

A

alkenes with a hydroxyl group

C=C-OH

312
Q

H NMR: split peaks calcuation

A

number of non-equivalent hydrogen neighbors (attached to an adjacent carbon) plus one

MCAT (3 decks)

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