Unit 1 Cells and Proteins: Key Area 2 Proteins (Structure) Flashcards

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1
Q

what is a distinguishing feature of proteins?

A

there folded nature and ability to bind specifically to other molecules.

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2
Q

what are proteins polymers of?

A

amino acids.

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3
Q

what are 2 functional groups of amino acids?

A

the amine and acid group

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4
Q

what does wide range of functions carried out by proteins result from?

A

the wide range of functions carried out by proteins results from the diversity of R groups.

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5
Q

what determines the structure of the protein?

A

the sequence of amino acids.

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6
Q

what makes each amino acid different?

A

the R group.

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7
Q

what are 5 components of amino acids?

A

the amine group, acid group, R-group, hydrogen atom and central carbon.

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8
Q

what are amino acids linked together by and what does this produce?

A

peptide bonds which produces a polypeptide.

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9
Q

what are the 4 main R-groups of amino acids?

A

polar, hydrophobic, acidic (negatively charged), basic (positively charged).

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10
Q

what can R-group of amino acids vary in?

A
size
shape
charge
hydrogen bonding
capacity
chemical reactivity
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11
Q

what are the key features of an acidic R-group?

A
  • ends with a negatively charged group
  • hydrophilic
  • key component is a carboxylic acid group
  • COOH
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12
Q

what are the key features of a basic R-group?

A
  • ends with a positively charged group
  • hydrophilic
  • key component of their R-groups is an amine group
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13
Q

what are the key features of a polar R-group?

A
  • slightly charged
  • hydrophilic
  • key component: carbonyl (CO), (OH), or amine (NH)
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14
Q

what are the key features of a hydrophobic R-group?

A
  • hydrophobic
  • do not have charge
  • non-polar
  • key component is a hydrocarbon - CH3, long chain of CH and rings
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15
Q

what are the other level of proteins structure other than the sequence and binding of amino acids?

A
  • Primary structure
  • Secondary structure
  • Tertiary structure
  • Quaternary structure
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16
Q

what is the primary structure?

A

the primary structure is the sequence in which the amino acids are synthesised into the polypeptide

17
Q

what happens in the primary structure?

A

amino acids link by peptide bonds to form a polypeptide

18
Q

what results in regions of a secondary structure?

A

hydrogen bonding along the backbone of the protein strand results in regions of secondary structure

19
Q

what are the 3 types of secondary structure?

A
  • alpha helix
  • beta sheets
  • turns
20
Q

how are alpha helix formed?

A

by twisting the polypeptide into a spiral/ helix then establishing with hydrogen bonds. where the R-groups stick out

21
Q

what are the 2 types of beta sheet?

A
  • parallel: the chains run in the same direction

- anti-parallel: the chains run in opposite directions

22
Q

what’s stabilises the alpha helix?

A

hydrogen bonding

23
Q

what is the tertiary structure?

A

further folding of secondary shapes into an overall three- dimensional shape

24
Q

how is the tertiary structure established?

A

by many different interactions between the R-groups of the amino acids