amino acids and proteins Flashcards

1
Q

how many amino acids are there

A

20

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2
Q

all amino acids have similar structures but..

A

varying side chains

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3
Q

proteins are useful to cells because: 6

A

1) enzymes
2) structural (muscle, bone)
3) transcription factors- transcription and translation
4) lipid bound proteins act as transport systems
5) interact with sugars - glycosidic single on CSM
6) providing recognition of other molecules (e.g. receptors, growth factors, antibodies)

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4
Q

chriality

A

central alpha carbon ha 4 different substituents

–> all amino acids accept glycine have mirror images- all are in the L form

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5
Q

nomenclature

A
  • end in -ine
  • 3 letters (Gly)
  • abbreviated to one latter- however more than one amino acid has a common starting letter e.g. phenylalanine= F
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6
Q

amino acids exist as

A

zwitterions (has positive and negative parts) at a neutral pH of 7

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7
Q

as pH increases

A

COOh grop is deprontonated and gives up proton

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8
Q

peptide bond formation

A

amino acids join together and lose a molecule of water- condensation reaction

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9
Q

two types of peptide bonds

A

cis and trans

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10
Q

which peptide bond is more common

A

trans is favourable to cis- however proline has cis peptide bonds

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11
Q

example of how flexible proteins are

A

on binding with iron, Lactroferrins undergoes a substantial change in conformation which allows other molecule to distinguish between iron friend iron bound forms

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12
Q

4 main groups of amino acids

A

1) hydrophobic T groups with non polar R groups
2) polar amino acids with neutral R groups, but charge not equally distributed
3) positive charge on amino acid and R group (at a certain pH)
4) negative charge on the amino acid and R groups (pH)

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13
Q

histidine

A
  • found in Active sites of many enzymes
  • only amino acid of pKA of near neutral
  • charge can be modulated by other amino acids, surrounding it in the 3d structure of the protein
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14
Q

cysteine

A
  • contains a free thiol (SH) group
  • covalent bond with another cysteine on the protein chain where they approach each other in a 3d structures

-this disulphide bond is the only covalent bond found to maintain structure

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15
Q

cystine

A

two cysteine joined by a covalent bond

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16
Q

glycne

A
  • no chirality
  • adds flexibility to proteins. where other side chains would be two bulky
  • side chain =H
17
Q

alanine

A
  • used in bio-synthesis of proteins

- non-polar

18
Q

proline

A
  • side chain bonds to the amine group
  • imposes tight restraints on the conformation of the protein
  • cis and trans peptide bonds
  • found in rigid proteins like collagen