Packet #13 Flashcards

1
Q

zwitterion

A

amino acid in the form that has a negatively-charged carboxylate group on one end and a positively charged ammonium group on the other.

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2
Q

zwitterion + acid

A

amino acid cation + water

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3
Q

zwitterion + base

A

amino acid anion + water

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4
Q

How to make a dipeptide

A
  • -OH group from carboxylic acid end of first amino acid and a -H from the amine end of the other amino acid
  • needs strong acid catalyst
  • results in a dipeptide.
  • bond between the carbonyl C and the -N is a peptide bond
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5
Q

primary protein structure

A
  • the sequence of amino acid residues in a protein
  • Example: Gly-Ser-Gly-Ala
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6
Q

Secondary protein structure

A
  • this refers to whether a segment of a protein chain is coiled into a helix or whether the chains are stacked more straightly into sheets
  • alpha-helix
  • beta-sheets
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7
Q

Tertiary protein structure

A

Refers to how several helical segments or sheet segments of the same polypeptide chain are arranged in space relative to each other

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8
Q

Quaternary protein structure

A

Some proteins are made up of more than one polypeptide chain. Quaternary structure refers to how the separate chains are arranged in space relative to each other

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9
Q

protein definition

A

a polypeptide that has a specific sequence of amino acid residues and does a specific job in the body.

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10
Q

amino acid residue

A

when amino acids combine they are amides so they can’t be called an amino acid; called amino acid residues.

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11
Q

amyloidosis

A

a disease characterized by the presence of amyloid proteins (Alzheimer’s abd Creutzfeld-Jakob Disease)

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12
Q

amyloid

A

a protein that is normally alpha-helical BUT has been misfolded into a ß-sheet

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13
Q

protein jobs

A
  • structure (keratin & collagen)
  • catalys (lactase, sucrase, pepsin. . .)
  • muscle contraction (actin & myosin)
  • transport & storage (hemoglobin & myoglobin)
  • immune system (antibodies)
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