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LGS > FIT quiz 1 > Flashcards

FIT quiz 1 Flashcards

1
Q

5 keys aspects of healthy lifestyle

A
  1. nourish
  2. move
  3. rest
  4. restore
  5. connect
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2
Q

5 components of fitness

A
  1. cardiorespiratory
  2. strength
  3. flexibility
  4. balance/agility
  5. body composition
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3
Q

functional movements

A
  • pulling
  • leaning
  • bending
  • twisting
  • squatting
  • pushing
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4
Q

stress response

A

mind perceives a threat which activates the sympathetic nervous system which triggers the release of catecholines (epinephrine, norepinephrine,dopamine) and cortisol

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5
Q

highly effective methods of study

A

self testing and distributed practice

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6
Q

moderately effective study methods

A

elaborative interrogation (asking why), self-explanation (asking how), interleaved practice (benefits those who are reasonably competent)

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7
Q

ineffective study methods

A

underlining/highlighting, rereading, summarization, keyword mnemonics

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8
Q

3 basic stages involved in memory

A
  1. encoding - (selective and elaboration), uses our sensese
  2. storage - passive
  3. retrieval - recall accurately
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9
Q

sensory information store

A

retain information long enough to decide what to do with it next; large capacity, small duration

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10
Q

short-term memory

A

retains for about 10-20 seconds unless rehearsed and about 7 chunks of information; forgetting is likely due to interference

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11
Q

long-term memory

A

episodic, procedural, semantic; subject to retrieval failure

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12
Q

procedural memory

A

memories that occur outside of awareness and are often measured using indirect memory tests. both mental and physical actions, responsible for implicit memories. ex. long division, hitting a baseball after several years

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13
Q

semantic memory

A

memories for facts and details that are not mentally experienced as events in one’s life, usually stored in networks where each concept is linked by relation, conscious memories of facts, involve neotic consciousness (knowing consciousness) ex. names or history events

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14
Q

episodic memory

A

for personally experienced events that occurred at a particular time and place, involve mentally reliving the event, involve autonoetic consciousness (self-knowing consciousness) ex. first kiss

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15
Q

important brain areas involved in memory

A

hippocampus (important for conversion of short-term memory to long-term memory), amygdala (emotional, fear), basal ganglia, neocortex, cerevellum (procedural, motor function)

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16
Q

fundamental principles of EBM

A
  1. optimal clinical decision making requires awareness of the best available evidence
  2. provides guidance to decide whether evidence is more or less trustworthy
  3. evidence alone is never sufficient to make a clinical decision
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17
Q

5 types of foreground questions in EBM

A
  1. therapy
  2. harm
  3. differential diagnosis
  4. diagnosis
  5. prognosis
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18
Q

define the components of a P.I.C.O. formatted questions

A

patients or population
intervention
exposure
outcome

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19
Q

explain acid-base properties of water, main contributing factors to pH, and how they’re calculated

A

H2O + H2O -> H3O+ + OH-
pH = -log[H+], Kw = [H+][OH-], pH = pKa + log[base/acid]
pH depends on presence of acids and bases.

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20
Q

5 types of noncovalent interactions

A

dipole-dipole, electrostatic or salt bonds, ion-dipole, hydrophobic, van der waals

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21
Q

noncovalent interactions determine the biological properties of biomolecules

A

water solubility, higher-order structures of macromolecules, binding interactions between molecules

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22
Q

key chemical features of biomolecules

A

(SCHNOP)
mostly covalent bonds, mostly organic, mostly large, isomerization (stereospecific)

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23
Q

3 main goals of metabolism

A

generate energy
synthesize macromolecules
maintain homeostasis

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24
Q

4 basic pathways of metabolism

A

fuel oxidative (catabolic)
fuel storage (anabolic)
biosynthetic (anabolic)
detoxification or waste disposal (catabolic)

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25
Q

euchromatin vs. heterochromatin

A

euchromatin is more open, rich with genes. heterochromatin is dense with little to no transcriptional activity

26
Q

nucleolus vs. nucleus

A

nucleolus is within the nucleus and is specifically where activity of protein synthesis occurs. more prominent and densely concentrated rRNA.

27
Q

steps of DNA replication

A
  1. helicase unwinds the parental double helix
  2. proteins (ex. topoisomerase) stabilize the unwound parental DNA
  3. leading strand is synthesized continuously by DNA polymerase
  4. lagging strand is synthesized discontinuously. RNA polymerase synthesizes a short RNA primer, which is then extended by DNA polymerase
  5. DNA polymerase digests RNA primer and replaces it with DNA
  6. DNA ligase joins the Okazaki fragments of the lagging strand
28
Q

when does replication happen

A

during S phase of cell cycle

29
Q

why does replication start at multiple points of origin

A

eukaryotes replicate much slower than prokaryotes to reduce possibility of mutations and because of the abundance of genes

30
Q

accuracy of DNA replication is due to what 3 factors

A
  1. proper nucleotide selection - ability of DNA polymerases to discriminate between correct and incorrect nucleotides
  2. proofreading - the ability of polymerase-associated exonucleases to remove incorrect nucleotides from the DNA immediately after their incorporation (polymerase beta)
  3. mismatch repair - DNA repair mechanism by which mismatched nucleotides in new strand are removed. occurs predominantly in S phase. defects in MMR are cause for lynch syndrome - previously known as HNPP
31
Q

polymerase alpha, beta, gamma, delta, epsilon functions and exonuclease activity

A

alpha - replication (in a complex with primase and aids in starting the primer), DNA repair. no exonuclease activity (EA)
beta - DNA repair exclusively. No EA.
gamma - DNA replication in mitochondria. EA: 3’-to-5’
delta - replication (processive DNA synthesis on lagging strand), DNA repair. EA: 3’-to-5’
epsilon - replication (processive DNA synthesis on leading strand), DNA repair. EAL 3’-to-5’

32
Q

nuclear excision repair (NER)

A

-single strand DNA repair mechanism
- specific endonucleases release the oligonucleotides containing damaged bases
- dna polymerase and ligase fill and reseal the gap
- repairs bulky helix-distorting lesions
- occurs in G1 phase of cell cycle
- defective xeroderma pigmentosum - inability to repair DNA pyrimidine dimers caused by UV exposure
findings: dry skin, extreme light sensitivity, skin cancer

33
Q

base excision repair (BER)

A
  • base-specific glycosylase removes altered base and creates AP site
  • one or more nucleotides are removed by AP-endonuclease, which cleaves 5’ end
  • AP-lyase cleaves 3’ end DNA polymerase-beta fills the gap and DNA ligase seals it
  • occurs throughout cell cycle
34
Q

non-homologous end joining

A
  • DNA repair mechanisms double strand
  • brings together 2 ends of DNA fragments to repair double-stranded breaks homologous end joining
  • can lead to lost or inserted DNA
  • defective in ataxia-telangiectasia
35
Q

homologous recombination

A
  • DNA repair mechanism double strand
  • requires 2 homologous DNA duplexes
  • a strand from damaged dsDNA is repaired using a complementary strand from intact homologous dsDNA as a template
  • defective in breast/ovarian cancers with BRCA1 mutation and in fanconi anemia
36
Q

posttranscriptional modification

A

adding 5-methyl-guanosine cap, polyadenylation tail, splicing by spliceosome and leaving the nucleus to bind to ribosome

37
Q

start and stop codons

A

AUG

UAG
UAA
UGA

38
Q

rRNA complex size in euk. vs. prok.

A

Euk: small 40S + large 60S = 80S
prok: 30S + 50S = 70S

39
Q

why does location of rRNA matter?

A

cytoplasmic rRNA processes mRNA for peptides that remain in the cell. RER rRNA translate for peptides destined either for the cell membrane or to be released outside of the cell.

40
Q

tRNA structure and function

A
  • CCA (can carry amino acids)
  • T-arm (tethers tRNA molecule to ribosome)
  • D-arm (allows detection of the tRNA by aminoacyl-tRNA synthetase)
41
Q

aminoacyl-tRNA synthetase

A

uses ATP to bind an AA and charge it. then pyrophosphate is released and the synthetase matches an AA to the tRNA by scrutinizing the AA before and after it binds to tRNA

42
Q

3 Pillars of Biochemistry

A

Biomolecules - all molecules found in living organisms
Metabolism - all chemical reactions that occur in living organisms
Molecular Biology - molecular mechanism of inheritance

43
Q

Enzymes Involved in Unwinding of DNA

A

Helicase
Single-stranded DNA binding proteins - helps prevent rapid degradation
Topoisomerases - prevents supercoiling while unwinding

44
Q

Telomeres

A
  • cap the end of chromosomes and consist of repeat sequences of TTAGGG
  • binding of shelterin proteins protect ends from damage
  • shorten with each replication
    Hayflick’s limit determines maximum times DNA can replication (mitotic clock)
  • telomerase is RNA dependent DNA polymerase like reverse transcriptase can extends of chromosomes
45
Q

Types of RNA polymerases

A

type 1 - transcribes rRNA, located only in nucleolus
type 2 - preRNA (hnRNA), miRNA, snRNA
type 3 - transcribes tRNA, 5S rRNA

46
Q

Aminoacyl-tRNA synthetase

A
  1. ATP and an amino acid bind to it to charge it
  2. pyrophosphate is released
  3. synthetase matches an amino acid to the tRNA
    *if correct AA, AMP is released, if incorrect, bond is hydrolyzed)
  4. charged tRNA is released from synthetase
47
Q

Translation Initiation Factors

A
  • elF2 binds to initiator tRNAi + GTP to 40S rRNA with help of elF3 (pulls everything together)
  • elF4E identifies 5’ cap via cap binding proteins (rate limiting step)
48
Q

Translation - Elongation

A

1st. Met binds to P site
2nd AA binds to A site
3rd. peptidyl-transferase catalyzed peptide bond formation -> transfers growing polypeptide to A site
4. 2nd AA tRNA moves to P side (translocation) which requires eEF-2 and GTP. this kicks out Met tRNA in E site
each cycle requires 4 phosphate bonds

49
Q

Translational Regulation - miRNA

A
  1. Cell makes hairpin miRNA and releases them from the nucleus - transported by exportin 5
  2. Hairpin loop removed and binds with chaperon proteins called argonuates
  3. miRNA binds with complementary strand of mRNA
  4. Destabilizes mRNA leading to miRNA induced mRNA decay
50
Q

Protein Folding - (primary, secondary,etc)

A

primary - sequence from N terminal to C terminal
secondary - structure based on hydrogen bonds within sequence (alpha helix vs. beta pleated sheets)
tertiary - reactions based on peptides amino side chains within sequence - often assisted by chaperone proteins
quaternary - combine with other peptides - leads to locus heterogeneity. formed mainly by hydrophobic interactions

51
Q

post-translational modifications

A
  • cleaved into smaller ones
  • modified by phosphorylation, glycosylation, hydroxylation, methylation, acetylation, and ubiquitination (Post grad has me and U)
  • given signals to leave or transport to specific organelles
52
Q

Acidic vs. basic amino acids

A

acidic (-) - Tyr, Cys, Asp, Glu
basic (+) - Arg, Lys, His
acidic pH - bases are ionized
basic pH - acids are ionized

53
Q

conjugated enzyme

A

protein (apoenzyme) and cofactor (coenzyme + prosthetic group)

54
Q

holoenzyme

A

catalytically active conjugated enzyme

55
Q

zymogen (proenzyme)

A

enzyme synthesized in a catalytically inactive form - requires metabolic processing to become active

56
Q

isoenzymes

A

different structural forms of an enzyme have the same function

57
Q

Prion proteins and associated diseases

A
  • misfolded becoming dysfunctional and are contagious - can lead to disease or cell death
  • Familial creutzfeldt-jakob disease (fCJD) - caused by sporadic or inherited mutations causing PrPSc formation
    -variant CJF - caused by consumption of meat acquired from “mad cow disease” - infected cattle
    Latrogenic CJD - caused by cadaveric human growth-hormone use
    Kuru - caused by consumption &/or improper handling of human tissues containing PrPSc
58
Q

Dissociation constant

A

Kd = [L][P]/[LP] = k-1/k1

59
Q

Uncompetitive inhibitor

A

both Km and Vmax decrease because it only binds to the [ES] complex, reversible

60
Q

Noncompetitive Inhibitor

A

Vmax decreased, Km unaffected, binds to only allosteric site, irreversible because it is covalently bound

61
Q

Competitive Inhibitor

A

Vmax unaffected, Km decreased, binds to substrate site, reversible

LGS (2 decks)

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