1.9 Into to Proteins Flashcards

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1
Q

What are proteins made of?

A

Long chains of amino acids

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2
Q

What is the structure of amino acids?

A

[from left to right]
NH2 attched to 2 C’s.
Middle C has an H at the top and an R group at the bottom.
C at the end is attached to a double bond O and an OH.

carboxyl, R-side chain, & an amino group

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3
Q

What are peptide bonds? Polypeptide chains?

A

Amino acids connected together using amide bonds. A string of these amino acids are called poly peptide chains?

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4
Q

What is the primary structure of a protein?

List points

A
  • proteins organized in the precise sequence of amino acids that appear in the polypeptide chain
  • starting point for determining the final structure of a protein
  • small substitutions can greatly affect the protein by altering its ability to function and could affect protein folding
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5
Q

Does the structure of a protein matter?

A

Yes
FUNCTION DETERMINES STRUCTURE
STRUCTURE DETERMINES FUNCTION

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6
Q

What is the secondary structure of a protein?

List points

A

Different parts of the chain begin to fold on itself.
In this stage, the chain will fold in one of three ways:
1) alpha-helix (similar to DNA but single stranded)
2) beta-pleated sheet
3) random coil
It’s all held together by hydrogen bonds

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7
Q

What is the tertiary structure of a protein?

List points

A
  • When the secondary structure folds even more around itself
  • many causes of this structure ex: H-bonding, hydrophilic/phobic interations, disulfide bridges (S-S), ionic boning, and proline kinks
  • structures can either be globular (ex. hemoglobin) or fiberous (ex. hair)
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8
Q

What is the quaternary structure of a protein?

Lists points

A
  • proteins can be made of more than one polypeptide chain
  • this is when the protein is folded around even more
  • not all proteins have a quaternary structure
  • interactions with other side chains here in this structure
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9
Q

What are chaperone proteins?

A

Special proteins that help primary polypeptide chains fold and develop into tertiary structures.
“molecular supervisors”

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10
Q

What is denaturation?

Protein denaturation

A

This occurs when proteins lose its shape, and therefore loses its function.
Sometimes this is temporary

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11
Q

What can cause denaturation?

Protein denaturation

A

Causes include:
- temperature
- change in pH
- exposure to radiation
(Ex: cooking eggs)

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12
Q

What are heat shock proteins (HSP)?
What do they do?

A
  • a group of chaperone proteins is called HSP
  • desgined to cling onto other proteins and prevent them from denaturation
  • usually a low concentration of HSP until a stress is detected, in which they rapidly replicate and surround the cell to protect it
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