biological molecules💧 Flashcards

1
Q

what happens in hydrolysis

A

water is added

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2
Q

how does salting preserve food

A
  • reduces wp outside bacteria

- bacteria lose water by osmosis and cannot reproduce

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3
Q

why is mRNA smaller than DNA

A
  • mRNA contains copy of one gene

- DNA contains many genes

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4
Q

differences between globular and fibrous proteins using hb and collagen

A

g- soluble

  • hydrophilic R group on outside
  • spherical
  • forms h bonds with water

hb-haem group
-transports oxygen

f-insoluble, strong

  • chains can form h bonds with adjacent chains
  • structural role
  • long chains

c-forms crosslinks between molecules
-connective tissue

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5
Q

r group interactions in tertiary structure

A
  • positive or negative charge forms ionic bonds
  • hydrophobic on inside
  • hydrophilic on outside
  • hydrogen bonds
  • disulfide bonds between sulfur atoms
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6
Q

explain how these properties help organisms survive in a pond

  • ice floats
  • solvent
  • lot of energy needed to break bonds
A
  • molecules spread out
  • lattice
  • water below ice does not freeze
  • organisms do not freeze and can move
  • polar
  • ions interact with water
  • organisms uptake minerals
  • high specific heat capacity
  • hydrogen bonds
  • lot of energy needed to break bonds
  • temperature does not change much so enzymes can function
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7
Q

where are hydrogen bonds found in biological molecules

A
  • water
  • tertiary structure of protein
  • a helix B pleated sheet
  • between bases in DNA
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8
Q

cholesterol function

A
  • energy storage
  • regulates fluidity of membrane
  • making vitamin D
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9
Q

why is glycogen good for storage

A
  • compact
  • high energy density
  • easily broken down
  • branched for enzymes to attach
  • insoluble
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10
Q

function of glucose

A
  • source of energy

- used for respiration

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11
Q

how is collagen similar to haemoglobin

A
  • amino acid chains
  • helix
  • more than 1 polypeptide
  • quaternary structure
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12
Q

describe structure of haemoglobin

A

-sequence of amino acids joined by peptide bonds

sec

  • a helix
  • hydrogen bonds

tert

  • polypeptide undergoes further folding
  • hydrophilic R group outside
  • disulfide, ionic, hydrogen bonds

quat

  • 4 polypeptides
  • 2 alpha chains 2 beta chains
  • 1 haem group per polypeptide

-prosthetic group haem contains Fe2+ ion

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13
Q

does cholesterol contain fatty acids

A

no lol

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14
Q

why can water form h bonds

A

-water molecule is polar as electrons are held closer to oxygen

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15
Q

what level of structure are alpha and beta sub units in

A

quaternary

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16
Q

why is waters solvent ability important

A
  • medium for metabolic reactions
  • organisms can take in minerals
  • transport
  • able to dilute toxic substances
17
Q

describe collagen structure

A
  • peptide bonds between amino acids
  • left handed helix
  • every third amino acid is glycine
  • 3 polypeptide chains
  • h bonds between polypeptide chains
  • adjacent molecules joined by crosslinks
  • crosslinks staggered
  • fibril
18
Q

properties of fibrous proteins

A
  • insoluble
  • strong
  • unreactive
19
Q

functions of fibrous proteins

A

protection, structure, elasticity, contraction

20
Q

how to extract dna

A
  • grind sample to break down cell walls
  • salt helps DNA precipitate
  • use detergent to break down nuclear envelope
  • add protease to break down histones
  • add cold ethanol to precipitate
21
Q

how to calibrate colorimeter

A

set to zero absorbance using water

22
Q

how to test for sucrose

A
  • heat with benedicts (should be blue)

- boil with HCL then retest with benedicts (red)

23
Q

structure difference between glycogen and amylopectin that makes glycogen a more suitable storage molecule

A

-glycogen more branched so can be broken down by enzymes faster
-branching gives more free ends where glucose can be added or removed
-glycogen more compact
-glycogen more coiled
-