L4 - Covalent And Non-covalent Bonding Flashcards

1
Q

What is ionic bonding?

A

The electrostatic interaction of the differently charged species

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2
Q

NaCl as an example of ionic bonding

A
  • in order to reach stability of a filled shell, it can gain an e- from a suitable source
  • when salt in solid form, ions are arranged in regular arrays
  • energy of the electrostatic interactions is partly why it’s stable
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3
Q

What is covalent bonding?

A

The chemical bond that involved the sharing of pairs of electrons between atoms

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4
Q

How do covalent bonds form?

A

Bring two atoms close together, the 2 atomic orbitals now merge into a single bond orbital that contains both electrons

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5
Q

What are important points about covalent bonds?

A
  • electrons must have opposite spins, must be paired
  • each electron is able to exist in any part of the bond orbital, belongs to both atomic nuclei
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6
Q

What is bond dissociation energy?

A

The energy needed to break the bond that was formed

A measure of how strong the bond is

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7
Q

What is hydrogen bonding?

A

A partially electrostatic attraction between a H which is bound to a more electronegative atom such as N,O,F and another adjacent atom bearing a lone pair of electrons

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8
Q

What does the strength of the hydrogen bond depend on?

A

The donor and acceptor atoms and their environments and geometries

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9
Q

What are the consequences of H bonding in small molecules?

A

Increase in melting point, boiling point, solubility and viscosity

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10
Q

What are Van der Waals forces?

A

Relatively weak forces that attract neutral molecules to one another

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11
Q

What are the three soureces that VdW arise from?

A
  • electrically neutral molecules may exhibit permanent electric dipoles
  • these dipoles have tendency to align = net attractive force
  • permanent dipoles may temporarily distort the electric charge in a neraby molecule
  • molecules with no permanent dipole temporarily dipoles from the random electron motion = london forces
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12
Q

What is pi-stacking?

A

Attractive, non covalent interactions between aromatic rings

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13
Q

What are the 3 recognised arrangements?

A
  • sandwhich
  • t shaped
  • parallel; displaced
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14
Q

What is the evidence for pi stacking?

A
  • gas phase and low temp benzene forms a dimer, binding energy
  • x-ray crystallography gives perpendicular and offset paraller configuartions in many simple aromatic compounds
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15
Q

What are hydrophobic interactions?

A

Describes the segregation of water and non-polar substances

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16
Q

What feature does water have that affects mixtures?

A
  • strong network of hydrogen bonds
    = non polar molecules cannot form hydrogen bonds
17
Q

What are amphiphiles?

A

Molecules both hydrophobic and hydrophilic domains

18
Q

What are amphiphilic molecules arranged like in micelles?

A

The hydrophilic head is found on the outside and the hydrophobic tails reside inside

19
Q

What are proteins? And give examples of amino acids with hydrophobic elements

A

Macromolecules

  • glycine
  • alanine
  • valine
  • leucine
  • phenylalanine
  • tryptophan
  • methionine
20
Q

Why are charged and polar residues found on the outside?

A

They can intereact with the surrounding water molecules

  • minimises the number of hydrophobic side chains exposed to the water solvation sphere
    = the principle driving force behind the folding process
21
Q

What are the protein structures?

A
  • primary
  • secondary
  • tertiary
  • quaternary
22
Q

What is the primary protein structure?

A

Sequence of amino acids in the polypeptide chain
- held together by peptide bonds
- formed from the acid group of one and the amine group of another

23
Q

What is the secondary protein structure?

A

Highly regular sub-structures on the polypeptide backbone chain (alpha helix, beta pleated sheets)
- pattern defined by hydrogen bonds
- between the main-chain peptide groups

24
Q

What is the tertiary protein structure?

A

Overall 3D shape of the protein molecules, 2nd structure folded into a compact globular structure
- driven by the non-specific hydrophobic interactions
- interactions such as salt bridges, hydrogen bonds, tight packing of side chains and disulphide bonds

25
Q

What is the primary structure started by?

A

The amino-terminal (N) end

26
Q

How are beta pleated sheets held?

A

Hydrogen bonds
- carbonyl of residue n interacts with the amide proton of residue n+4

27
Q

How many residues do alpha and beta need in the secondary structure?

A

Alpha - 5.4
Beta - 3.6

28
Q

How are tertiary and quaternary structure?

A

Hydrophobic effect is the main driving force in the protein folding
- hydrophobic residues forced into core of the forming globular sturcture, hydrophilic remain at the surface
- energy gain = vdw in the hydrophobic region = stability of folded protein
+ pi-stacking, salt bridges and disulphide bonds