biomolecule revision Flashcards

1
Q

Covalent bonds

A

formed by sharing of electrons

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2
Q

single covalent bonds

A

share 2 electrons between atoms

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3
Q

double covalent bonds

A

share 4 electrons & stronger than single covalent bonds

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4
Q

polar covalent bonds

A

unequal sharing of electrons producing a postive charge at one end of the molecule, and a negative charge at the other end = net dipole

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5
Q

non polar covalent bonds

A

equal sharing of electrons & no net dipole

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6
Q

whats stronger covalent or non covalent bonds

A

covalent bonds

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7
Q

types of non covalent bonds

A
  1. thermal energy
  2. can der waals
  3. hydrogen bonds
  4. iconic bonds
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8
Q

ionic bonds

A

occur between two opposite charged ions & involve the complete transfer (either gained or loss) of electrons

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9
Q

how are ionic bonds weakened

A

by water, water can cluster around charged ions to weaken the interaction

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10
Q

what compounds formed by non covalent bond is soluble in water

A

ionic bonds e.g. NaCl = table salt

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11
Q

hydrogen bonds

A

occur due to attraction of positively charged H atoms to negatively charged atoms

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12
Q

how are hydrogen bonds weakened

A

water, as water competes for H bond interactions

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13
Q

hydrophobic forces

A

occur due to the attraction between non polar molecules & exclusion of water

water molecules cannot form hydrogen bonds with non polar molecules & tend to form pentagon or hexagon cages around the non polar molecules instead

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14
Q

molecular complementarity

A

Multiple non-covalent interactions can form between complementary molecules causing them to bind.

It can be thought of as a lock and key fit between molecules whose shape and charge are complementary to each other.

E.g. molecular complementarity and non-covalent bonds are what holds two DNA strands together into a double helix.

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15
Q

Van der Wall forces

A

attraction of neutral molecules in gases e.g. hydrogen bonding = weak bond formal transient dipoles

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16
Q

amino acid structure

A

determines the properties of the protein

17
Q

amino group

A

designates the N terminus of a protein. has a positive charge when ionised.

18
Q

carboxyl group

A

this designates the C terminus of a protein. has a negative charge when ionised

19
Q

which isomer is most common in proteins found in humans

A

L isomers NOT D isomers

20
Q

where do peptide bonds occur

A

between carboxyl group of one amino acid & amine group of another amino acid

21
Q

what does a peptide bond result in molecular wise

A

results in ned loss of one H molecule (from N terminus) & one OH molecule (from C terminus) in a process called a dehydration or condensation reaction (net loss of one water molecule)

22
Q

primary structure

A

linear sequence of amino acids formed by peptide bonds into a polypeptide chain

23
Q

secondary structure

A

organisation of the polypeptide chain in a alpha helix or b sheets or turns. structures are stabilised by hydrogen bonds between backbone of the amino acids

24
Q

tertiary structure

A

arrangement of secondary structures

25
Q

quaternary structures

A

number of polypeptide chains that is stabilised by non-covalent bonds in a multimeric protein

26
Q

two types of nucleic acids

A

deoxyribonucleic acid

ribonucleic acid

27
Q

nucleotides consist of

A

sugar molecule, attached to a phosphate group &. a nitrogen containing base

28
Q

phosphodiester bonds

A

joins nucleotides into a chain to form nucleic acids

  • between the hydroxyl group of phosphate with the sugar molecule (C3) & the hydroxyl group of the same phosphate with another sugar molecule (C5)
29
Q

nucleic acid

A

multiple nucleotides

30
Q

difference between saturated & unsaturated

A

saturated - no double bonds, higher boiling point, solid at room temp

the longer the chain the less double bonds, the higher the melting point

31
Q

transfat

A

c not z

hydrogens same side of double bond

32
Q

formation of triglycerides reaction name

A

condensation

33
Q

are phospholipids amphipathic & importance

A

yes, cell membrane

34
Q

bonds of

  1. nucleic acids
  2. proteins
  3. carbs
  4. glycerol & fatty acids
A
  1. phosphodiester bonds
  2. peptide bonds
  3. glycosidic bonds
  4. ester bonds