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CHEE 370 > Midterm > Flashcards

Midterm Flashcards

1
Q

how does the cell membrane maintain life

A

uses selective permeability to maintain gradients and inequilibrium

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2
Q

metabolism (catabolism vs anabolism)

A

all chem reactions that maintain cell life.

catabolism: breakdown of molecules to obtain energy
anabolism: synthesis of all compounds need by cell

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3
Q

attributes of all living organisms (7)

A

cell membrane, metabolic processes facilitated by enzymes, spend energy, react to stimuli, reproduction, mutability, non-equilib (selective permeability)

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4
Q

stereoisomer, chiral center, enantiomer

A

stereoisomer: 2 molecules w same formula and f.g. but cannot be superimposed
chiral center: center of asymmetry
enantiomer: mirror image

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5
Q

end of monosacharride

A

carbon of aldehyde or ketone (lowest number convention)

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6
Q

reaction of monosaccharide

A
  1. reaction with aldehyde or ketone (hemiacetal/hemiketal product)
  2. linear to ring structure forms
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7
Q

glycosidic bond

A
  • dehydration synthesis reaction
  • join monosacc/longer sugar chains
    forms di,oligo,polysaccharides
  • in acidic environment
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8
Q

central dogma of molecular biology

A

DNA-(transcription)->RNA-(translation)->protein (amino acid)

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9
Q

nucleotide vs nucleoside

A

nucleotide: sugar ribose+base+phosphate
nucleoside: sugar ribose+base

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10
Q

nitrogenous bases (5)

A

pyrimidine: C, T (DNA), U (RNA)
purine: A, G

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11
Q

define deoxy-ribo-nucleic-acid

A

deoxy: without oxygen on 2’ carbon of ribose
ribo: ribose sugar
nucleic acid: nucleotide
acid: acidic phosphate group

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12
Q

why does DNA have double helix?

A
  • strands oriented is opposite direction
  • complementary base pairs
  • H bond bw bp
  • VDW bw stacked bases
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13
Q

heterochromatin vs euchromatin

A

hetero: when cells not dividing (interphase), chromosones are more packed
euchro: less condensed (in prokaryotes)

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14
Q

denaturation, annealing, melting

A

denat: DNA strand seperation, w/ or w/out T chnage
annealing: upon cooling, some/all complementary strands re establish
melting: seperation above given T

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15
Q

DNA melting curve, DNA melting temperature

A
  • dna absorbs more light when it denatures

- T as which slope of absorbance is steepest

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16
Q

result of RNA annealing

A
  • forms double helical and complex 3D structure
  • tRNA (transfer)
  • rRNA (ribosome)
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17
Q

tRNA vs rRNA

A

tRNA: 3D cloverleaf created by local annealing of nucleotides
rRNA: 3D in ribosome, part of catalytic rxn to make protein (active site of ribosome)

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18
Q

interactions that stabilize DNA (4)

A
  1. hydrophobic effect
  2. H bond bw bp
  3. base stacking
  4. ionic int bw neg phosphate backbone and ions in solution
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19
Q

peptide bond

A
  • between carboxyl and amino group

- condensation/dehydration synthesis

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20
Q

pKa and acidity

A

pKa incr, Ka decr, acidity decr

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21
Q

pH>pKa vs pH

A

pH>pKa (basic): fg deprot ie acts as acid

pH

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22
Q

buffer selection

A
  • capacity highest when pH=pKa

- low slope regions: low pH changes

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23
Q

isoelectric point

A

pH at which the average charge of a solution containing the amino acid is neutral

24
Q

secondary structure

A
  • h bond within backbone of one strand
  • alpha helix
  • beta sheet (parallel vs antiparallel)
25
tertiary structure
organisations of series of secondary structure elements (h bond, hydrophobic, polypetide backbone, disulfide bridge, ionic bond)
26
disulfide bond
- 2 cyteines in close proximity form covalent bond | - stabilizes tertiary structure
27
quaternary structure
each peptide chain is a protein subunit
28
motif
- small regions of 3D structure/AA sequence shared among proteins - conserved - unique function
29
fold
orientations of motifs within tertiary protein structure
30
domain
- conserved sequence pattern - independent functional and structural unit - longer than motifs
31
classes of proteins (3)
1. globular (transport) 2. fibrillar (structure) 3. integral (receptor)
32
glycosylation
- protein-saccharide link - covalent - takes place in ER and golgi - can change protein half life
33
types of glycosylation
1. N-link: occurs on side chain of Asn | 2. O-link: occurs on side chain of Ser or Thr
34
triacylglcerols (triglycerides)
- fat - acid, hydrocarbon, alc - high energy
35
glycerophospholipids (phosphoglycerides)
- one of hydroxyl groups of glycerol is occupied by phosphodiatic head - amphiphilic: molecule w/ polar and non polar regions
35
glycerophospholipids (phosphoglycerides)
- one of hydroxyl groups of glycerol is occupied by phosphodiatic head - amphiphilic: molecule w/ polar and non polar regions
36
sphingo-lipids
- phosphate group can be switched w/ OH | - glycerol backbone is bound by amine or amide
37
saponification
triglyceride+NaOH= | glycerol+soap molecule
38
steroids
- slightly amphiphilic due to OH | - rigid ring structure provides rigidity to membrane
39
diffusion (2 types)
transverse: flip flop, slow lateral: fast
40
transition temperature
- from solid to liquid of phosphlipid bilayer - gel like solid: T below Tt - liquid crystal: T above Tt
41
factors affecting transition temp
1. chain length | 2. number of double bond
42
liposomes
- phospholipid as drug delivery vehicle | - entry routes of liposome into cell: receptor specific endocytosis, adsorption
43
gram positive vs negative bacteria
- peptidoglycan: thick in (+) - membrane structure: (-) have 2 membranes (inner, outer) - lipopolysaccharides: (-)
44
LPS
- outer membrane bacteria (-) - lipids with polysaccharide chain - trigger immune reactions in animals against pathogenic bacteria
45
enzymes
- large proteins that catalyze rxn | - do not change G, but change time needed for rxn
46
enzyme anatomy
- scaffold to support and position active site - binding site: bind and orient substrate - catalytic site: reduce Ea
47
theories of enzyme binding (2)
1. lock and key | 2. induced fit
48
cofactors and coenzymes
- used by enzymes to complete met. rxn cofactor: inorganic ions (metals) coenzyme: organic molecules
49
enzyme functions (5)
1. acid base catalysis 2. covalent catalysis 3. metal ion catalysis 4. electrostatic catlysis 5. proximity and orientation effects
50
Km
substrate concentration that provides a reaction velocity that is half the max velocity under saturating substrate conditions
51
turnover number (kcat)
- measure if catalytic act - # substrate molecules converted to product/enzyme molecule/time - if MM: k2=kcat=Vmax/Et
52
catalytic efficiency (kcat/Km)
- estimate of how perfect enzyme is | - measures enzyme performance when S is low
53
Lineweaver-Burk diagram
double reciprocal plot of 1/[S] vs 1/V - slope=Km/Vmax - yint=1/Vmax
54
enzyme inhibition
- regulatory mechanism | cells: change enzyme concentration, regulate activity of enzymes
55
types of inhibition (3)
1. competitive: Km incr 2. uncompetitive: Km, Vmax decr 3. mixed inhibition: Vmax reduced
56
specific activity of pure enzyme
units: micromoles/min/mg of enzyme

CHEE 370 (5 decks)

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