nucleic acids and protein structure Flashcards

1
Q

what determines macromolecular structure?

A
  • covalent bonds
  • electrostatic interactions
  • hydrogen bonds
  • hydrophobic interactions
  • van der waals forces
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2
Q

what is covalent bonding?

A

sharing of electrons between hydrogen bonds. the strongest type

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3
Q

what is ionic bonding?

A

bond formed between charged groups with opposing charges

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4
Q

why are ionic bonds on the surface of a protein weaker than ionic bonds within a protein?

A

on the surface of a protein, charged groups are very common

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5
Q

what is hydrogen bonding?

A

electrostatic interactions between an electron lone pair and an acidic proton

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6
Q

what are hydrophobic interactions?

A

repulsion of hydrophobic molecules from water, to allow water to maximise hydrogen bonding and maximise entropic potential

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7
Q

what are van der waals forces?

A

non-specific attractive force when 2 atoms are in close proximity

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8
Q

what does a nucleotide consist of?

A

a ribose sugar, base and 5’ phosphate

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9
Q

in what form is DNA found, in watson + crick base pairing?

A

B form; a right-handed double helix where phosphates form a charged surface

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10
Q

what is hoogsteen base pairing?

A

where thymine forms additional base pairs

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11
Q

what is a G-quadruplex?

A

four guanines, with usually a K+ ion in the middle

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12
Q

what type of helix does RNA form?

A

an A form helix

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13
Q

why can RNA form complex structures?

A

due to extra hydroxyl group on the ribose

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14
Q

what drives the formation of helices as a secondary structure?

A

favourable enthalpic interactions between amino acids with the backbone 4 residues away. plus a network of hydrogen bonds, which organise the helix to be stable

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15
Q

what is the difference between a B-strand and B-sheet?

A

in a B-strand, there is one peptide backbone in a straight conformation, whereas in a B-sheet there are many

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16
Q

what is a recognisable structural motif? give examples

A

a configuration which is recognisable between structures e.g. EF hand, leucine zipper, helix-turn-helix and 4 helix bundle

17
Q

how is a beta sheet formed?

A

linking 2 or more B-strands lying next to each other by hydrogen bonds

18
Q

what is the effect of turns and loops?

A

these structures are often rigid and well defined, and are found on the surface of proteins, interacting with other molecules

19
Q

how does the polypeptide chain fold in an aqueous environment and why?

A

folds so that hydrophobic groups are buried and its polar charged chains are on the outside. a system is more thermodynamically stable when hydrophobic residues are clustered together rather than extend into aqueous environment

20
Q

what is an intrinsically unstructured protein? what residues are common and uncommon amongst them?

A

a protein which completely or in part, has no discrete three-dimensional structure under physiological conditions. these regions are rich in charged and polar amino acids with few hydrophobic residues