Biochem Flashcards

1
Q

draw glucose galactose and fructose

A
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2
Q

draw sucrose, maltose, and lactose

A

sucrose: fructose + glucose
Maltose: glucose+ glucose
lactose: galactose + glucose

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3
Q

polysaccharadie/ oligosacchardie

A

-hundreds/thousands of repeating monosaccardesi
-broken down my brydrolyss for energy when needed
- in natural grains, takes longer to digest
- 2 types

  • short chains of monmers most cases theyre chains of glucose
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4
Q

storage polysaccharadie

A

starch
- glucose polymer
- found in plants, roots fruits
- like banas

glycogen
- glucose polymer, extensively brankced
- in animals, (liver msucles) clsoe to wher eyou need quick energy
- liver breaks things down

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5
Q

amino acids (draw basic structure)

A

protein building block
dehydration reaction creates polypeptide

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6
Q

polypeptide

A

Peptides are short chains of amino acids linked by peptide bonds.

formed from dehydratio reaction

also proteins

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7
Q

protein

A

chain of amino acids

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8
Q

1 2 3 4 protein structure

A

primary
- sequence of a chain of amino acids, unfolded

secondary
- local folding of the polypeptide chain into a helices and b pleated sheets

tertiary
- three dimensional foling patterin of a rpotein due to side chain interactions
- ca helix + B pleasted sheets combination sometimes

quat
- protein cosnisting of mroe then one amino acid chain (hemoglobin)
- several chains
-complicated moelcuels

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9
Q

fats

A
  • composed of smaller molecyels called glycerol and fatty acids
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10
Q

lipid

A

fat oils non polar, wax, steroids
-biololecules that dissolve in on-polar solid
- all NONPOLAR
- ususeful for energy storage, cellular structure (like membranes), insulation, and signaling.

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11
Q

phospholipid

A

hydrophobi
- has phosphate group head, fatty acid tail
- main component of cell membrane
-controls permeability of substances through membrane

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12
Q

triglyceride (be able to draw basic structure example)

A
  • glycerorl backbone
  • hydrophobic tail (fat)
  • hydrophilic head (acid)
  • ## inslatrion and energy storage (not very soluble)
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13
Q

fatty acid

A

long saturated/unsautyresd carbon cahirn terminating in carboxilic acid

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14
Q

glycerol backbone

A
  • simple moelcule found in glycerol lipid
    -deydrationr eaction attach 3 FA to 1 glycerol ester linkages
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15
Q

saturated fats

A

=BAD fats
- tightly packed, dense triglycerides
from animal fats, solid at room temp
-mono satutrated fats: one alkene bond

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16
Q

unsaturead fats

A

Good and Worst fats
- mostly derived from plants, liquid at room temp
- cis fats = good (salmon, anchovies, walnuts, corn oil, sunflower oil, Brazil nuts, and flax oil.)
-trans fats =worst (margarine, vegetable shortening, Vanaspati ghee, fried foods, and baked goods such as crackers, biscuits and pies)
- trans fat same structure as saturated fat but doubek bond makes it even harder to digest

17
Q

lipids vs carbs

A
  • simlialrities: good soruce fo energy, from plants

carbs
- polar
- quick easy simple source of energy (pirmarily used)
-mostly from plant

lipids
-non polar
- from vegatabels and animals
- slow dealyed source of ATP
- not broken down easily and mostly for storage, insulation, cell structure

18
Q

what is an enzyme

A
  • protein that acts as a catalyst for biological reactions
    -lower activation energy
19
Q

exergonic vs endergonic

A
  • basically exo thermic and endo thermic reactions and graphs
20
Q

substrate and steps to enzyme activity

A

-substance on which an enzyme acts
- enzyme structure complex that they act on SPECIFC substrates
- active sites on enzyme: where subrtate binds

steps
1. enzyme available with empty active sites
2. substrate binds to enzyme with induced fit
3. substrate is converted to products (dehydration reaction) like split sucrose
4. products (monosacchardies are relased

21
Q

Lock and key enzyme model

A
  • substrate fits into active site
  • reaction intermediate is formed
22
Q

induced fit enyme model

A
  • active site ins influenced by presance of substrate
  • CHANGES to accomodate it and form reaction intermediate

reaction intermidate:substrate + enzymes has decreased activation energy then reaction between reactants without catalyst

23
Q

enzyme reaction intermediate

A
  • products form
24
Q

factors influencing activity

A
  1. temeprature:
    -increase = increase Ek = increase collions = reaction rate
    - to much of an increase can lead to denature of enzymes (cuz their proteins)
    (look at graph)
  2. Ph
    - amino acods have acidic and basic parts
    - if ph changes protein will react with acids/bases in surroundings
    - so enzyme has to stay within oiptiam ph range or it denatures
    - differnt enzymes = diffenrt optiamal ph
  3. substrate concentration
    - increase [subsrtate] = increase reaction rate
    - reaction rate is limited by available active sites
    - when all enzymes occupied, its saturated
    (graph)
25
Q

cofactors and coenzymes

A

cofactors
non-protein chemical required for pptimal enzyme activitu
-includes inorganic molecules (metal ions, viatmons) and coenzymes

coenzymes
- organic cofactor that hpld onto useulf reaction components
- possible components being held could be the enzyme, substrate or another cofactor
-

26
Q

other factors influencing activity of enzymes (inhibition and cofactors)

A
  1. competeive inhibition
    - substrate like moelule blocks enzymatic action on actual substrate
  2. non compettive inhibition
    - moleule binds enzyme, altering its shape and activtiyu (allosteric inhibition)
  3. end product inhibition
    - downstream product allosterically inhibits early enzyme activity (makes profuct to inhibit enzyme)

non metal ions:
- they can improe the function of a protein but if theire presnet in to high a concentrtaion tehy can dentaure it, because they habe charges