Amino Acids and Proteins Flashcards

1
Q

3 Major Groups of Amino Acids

A

-non-polar
-polar
-electrically charged amino acids

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2
Q

2 types of electrically charged amino acids

A

acid and base

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3
Q

end of amino acid that has an unbound amino group

A

amino terminus (N-terminus)

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4
Q

end of amino acid that has unbound carboxyl group

A

C-terminus

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5
Q

peptide bond

A

bond between the C in the COOH of one amino acid and N in the NH2 of the next amino acid

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6
Q

primary structure

A

-sequence of amino acids in a polypeptide chain determined by gene that encodes for that protein

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7
Q

Secondary structure

A
  1. a helix
  2. B pleated sheets
    H bonding of the peptide backbone causes the amino acids to fold into repeating pattern
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8
Q

a helix

A

-often on the exterior of protein and involved in interactions with other molecules
-H bonds between every 4th amino acid

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9
Q

common types of tertiary interactions

A
  1. Hydrophobic interactions: amino acids with nonpolar, hydrophobic R groups cluster together on the inside of the protein, leaving hydrophilic amino acids on the outside to interact with surrounding water molecules.
  2. disulfide bridges: - covalent linkages between the sulfur-containing side chains of cysteines
    - act like molecular “safety pins,” keeping parts of the polypeptide firmly attached to one another
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10
Q

protein consisting of more than 1 amino acid chain

A

quarternary structure

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11
Q

Ways to Represent a Protein

A
  1. ribbon model of lysozymes
  2. space-filling model of lysozyme
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12
Q

ribbon model of lysozymes pros and cons

A

Pros
- very good at showing the secondary structure
- show functional units of protein

Cons
-can’t show us a realistic representation of what this protein looks like

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