Amino Acids and Protein Structure Flashcards

1
Q

what amino acids contain a hydroxyl group that can be replaced by a phosphoryl group

A

serine, threonine, tyrosine

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2
Q

what is glycolysation

A

addition of chains of sugars

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3
Q

what amino acids can undergo glycolysation

A
  1. Serine and threonine (O linked glycolysation)

2. Asparagine (N linked glycolisation)

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4
Q

what amino acid can a hydrocarbon chain be added to

A

cysteine because of its reactive sulfhydryl group

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5
Q

what amino acids have acidic side chains

A

glutamic acid and aspartic acid

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6
Q

what will a titration curve of an acidic AA chain look like

A

THREE buffering zones

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7
Q

what are the basic AAs

A

histidine, lysine, arginine

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8
Q

what bonds join proteins

A

peptide bonds between amino and carboxyl group

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9
Q

primary structure

A

linear order of AA starting at amino terminus

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10
Q

alpha helix produced by

A

hydrogen bonds forming between atoms in peptide bonds of a single linear chain

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11
Q

beta sheet produced by

A

hydrogen bonds forming between atoms in peptide bonds of the same or different linear chains
SAME: parallel
DIFFERENT: anti parallel

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12
Q

tertiary structure

A

overall 3D conformation determined by AA sequence. Peptide bond backbone and amino side chains determine this. H BONDS, IONIC BONDS, VAN DER WAALS

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13
Q

how do you get covalent interactions in AA side chains

A

two cysteines undergo formation of a covalent disulfide bond to make cysteine residue

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14
Q

domain

A

particular region of a protein with specific structure and function

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15
Q

quarternary structure

A

arrangement of protein subunits in complex that contains more than one polypeptide

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16
Q

what about proline limits the conformation

A

the ring (which is NOT aromatic)

17
Q

fatty acetylation

A

attach to a sulfur group

18
Q

4 helix bundle

A

hydrophobic core stabilized by ionic interactions

19
Q

tim barrel

A

8 alpha helices and 8 parallel b strands

20
Q

non globular proteins

A
  1. coiled coil (keratin)
  2. instrinsically disordered - few hydrophobic which is what drives folding - not stable at physiological conditions but very important regulators