2.2.9 proteins 2: protein structure & bonding Flashcards

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1
Q

primary structure

A

sequence of amino acids found in molecule

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2
Q

secondary structure

A
  • coiling/folding of amino acid chain (often due to h bond formation between different parts of chain)
  • main form: alpha helix or beta pleated sheet
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3
Q

tertiary structure

A
  • overall 3-dimensional shape of a protein molecule
  • due to interactions eg. h bonding, disulphide bridges, ionic bonds & hydrophobic interactions
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4
Q

quaternary structure

A

protein structure where protein consists of 1+ polypeptide chain

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5
Q

what does the order of amino acids in the primary structure determine

A

shape of protein molecule (through 2nd, 3rd, 4th structure)

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6
Q

what’s the alpha helix held by in the secondary structure (& between what)

A
  • hydrogen bonds
  • between -NH group of 1 amino acid & -CO group of another 4 places ahead in chain
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7
Q

what holds the beta pleated sheet together

A
  • hydrogen bonds
  • between the -NH group of 1 amino acid & -CO group of another further down strand
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8
Q

how are the alpha helix/beta pleated sheet made stable structures at optimal temp. & pH

A

due to the amount of hydrogen bonds formed

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9
Q

how is the precise shape of the tertiary structure held together

A

bonds between amino acids (which lie close to each other)

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10
Q

what may the tertiary structure adopt

A
  • supercoiled shape (fibrous proteins)
    OR
  • spherical shape (globular proteins)
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11
Q

what bond primarily holds the secondary structure

A

hydrogen bonds

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12
Q

what do hydrogen bonds form between

A

hydrogen atoms with slight positive charge & other atoms with slight negative charge

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13
Q

in amino acids, where do the h bonds form

A

form in hydroxyl, carboxyl & amino groups

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14
Q
  • where can ionic bonds form?
  • what do these ionise into?
A
  • between carboxyl & amino groups that are part of R groups
  • ionise into NH3+ & COO- = strongly attracted to each other
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15
Q

what does the R group of the amino acids cysteine contain

A

sulfur

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16
Q

where are disulfide bridges formed

A

between R groups of 2 cysteines

17
Q

what are disulfide bridges

A

strong covalent bonds

18
Q

where are the hydrophobic parts of the R groups found

A

usually associate together in centre of polypeptide

19
Q

where are the hydrophilic parts of the R group found

A

edge of polypeptide - close to water

20
Q

what causes twisting of the amino acids chain

A

hydrophobic & hydrophilic interactions

21
Q

what does this twisting of the amino acids chain cause

A

changes shape of protein