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BIO130 > Lecture 2 > Flashcards

Lecture 2 Flashcards

1
Q

what are the four steps of protein formation?

A
  1. primary
  2. secondary
  3. tertiary
  4. quaternary
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2
Q

what are proteins made of?

A

amino acids

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3
Q

what is the part that varies within amino acid structures?

A

the R group

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4
Q

what are the four main categories of amino acids?

A

acidic, basic, nonpolar, and uncharged polar amino acids

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5
Q

which type of amino acids makes disulphide bonds?

A

cysteine

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6
Q

how are peptide bonds formed?

A

when the oxygen of a carboxyl group of one amino acid reactions with the hydrogen of the amino group of an adjacent amino acid

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6
Q

what are the ends of polypeptide chains like?

A

an N terminus or amino group on one end and a C terminus or carboxyl group on the other end

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7
Q

why does the difference in primary amino acid sequences matter?

A

the unique sequence determines the unique structure and function of a protein

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7
Q

what is an alpha helix?

A

a spiral staircase protein structure

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8
Q

how are the hydrogen bonds in the alpha helix formed in terms of carbon number?

A

between every four amino acids

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9
Q

what are beta pleated sheets?

A

a flat arrangement of amino acids

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10
Q

how are hydrogen bonds formed in alpha helixes?

A

the hydrogen of one amino acid reacts with the oxygen in the carbonyl of an adjacent amino acid on the same strand

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11
Q

what are the R groups like in beta pleated sheets?

A

they alternate pointing up and down

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12
Q

what does antiparallel mean?

A

when the amino acids on one strand run in one direction and the amino acids on another strand run in the opposite direction

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12
Q

what are the two types of beta-pleated sheets?

A
  1. anti parallel
  2. parallel
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13
Q

what does parallel mean?

A

amino acids on both strands run in the same direction

14
Q

how are hydrogen bonds formed in beta-pleated sheets?

A

the hydrogen of one amino acid reacts with the oxygen in the carbonyl of an adjacent amino acid on the opposite strands

14
Q

what is the coiled coil?

A

when structures of alpha helixes wind around one another

15
Q

what is the property of coiled coils?

A

amphipathic

16
Q

what does amphipathic mean?

A

a molecule that has both hydrophobic and hydrophilic parts

17
Q

what is the tertiary stage of protein formation?

A

a 3D folded structure of a protein

18
Q

what forces hold the tertiary structure together?

A
  1. hydrophobic forces
  2. non-covalent parts
  3. disulphide bonds
19
Q

what are non-covalent bonds?

A

bonds within a protein formed by weak attractions

20
Q

what are hydrophobic interactions?

A

part of the protein that fears water

21
Q

what are disulphide bonds?

A

a bond that forms between the sulphur of two cysteine groups in two different amino acids

22
Q

why do proteins fold in a certain way in terms of energy?

A

they fold in a certain way that makes them most energetically stable

23
Q

what proteins help in the shaping process of making proteins?

A

chaperone proteins

24
Q

how many domains do eukaryotic proteins have?

A

two or more

25
Q

what are protein domains?

A

a specialized part of the tertiary structure that is semi-independent

26
Q

what are domains in eukaryotic proteins connected by?

A

intrinsically disordered sequences

27
Q

what are protein families?

A

proteins that have similar amino acid sequences and 3D structures

28
Q

how do protein domains play a role in protein evolution?

A

protein domains can be rearranged and altered during protein evolution

29
Q

what do proteins in protein famlies do in terms of evolution?

A

evolve to have different structures

30
Q

how are proteins in protein families similar in terms of domain structure?

A

they have similar domain structures even though they might have different overall structures

31
Q

what is hemoglobin made of?

A

two subunits, 2 alpha and 2 beta

32
Q

what are examples of different multiprotein complexes?

A
  1. actin filament;; structure with the same subunits
  2. viruses and ribosomes: structures made from different protein and DNA
  3. molecular machines; structures made of many different proteins to perform complex tasks
32
Q

What is each subunit like in hemoglobin?

A

the subunits function independently

32
Q

what are ways to study a protein in terms of purification?

A

electrophoresis and chromatography

33
Q

what is a way to study the protein in terms of amino acid sequences?

A

mass spectroscopy

BIO130 (6 decks)

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