Proteins Flashcards

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1
Q

protein function?

A

determining physical traits, behavior, and physiology

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2
Q

protein structure

A

amino acid chains connected by polypeptide bonds

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3
Q

Chemical structure of amino acids

A

Central Carbon
Amino group (NH2) base
Carboxyl group (COOH2) acid
Hydrogen atom- (H)
R-groups / side chains contain functional groups
Can participate in chemical reactions

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4
Q

Formation of peptide bonds

A

A peptide bond is a C-N covalent bond resulting from a condensation reaction (water is formed)

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5
Q

Primary structure

A

the sequence of amino acids

Each protein sequence is unique
A single aa change can radically alter protein function

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6
Q

Secondary structure

A

hydrogen bonds between carbonyl group of one aa and amino group of another

Electronegative oxygen and nitrogen atoms leave hydrogen atoms with partial positive charges.
α-helix twist
β-pleated sheet folding in on itself

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7
Q

Tertiary structure

A

Bending and folding into 3-dimensional shape of polypeptide

Results from interactions between residues causing the backbone to bend and fold
Bonds between sulfur atoms
Hydrophobic interactions
Hydrogen bonds
Ionic bonds

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8
Q

Quaternary

A

bonding of 2+ distinct polypeptide subunits

Dimers- proteins w 2 polypeptide units
Homodimers- 2 identical subunits
Heterodimers- non identical subunits
Tetramer- 4 polypeptide chains

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9
Q

Explain what prion diseases are and know the Kuru example

A

Prions are when proteins folding are altered. Misfolding is infectious and spreads throughout proteins

Kuru “laughing disease”
spread through eating brains of deceased

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10
Q

hydrogen bonding effect in folding

A

polar side chains and opposite partial charges

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11
Q

hydrophobic interactions in folding

A

water forces hydrophobic side chains together

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12
Q

Van Der Waals interactions in folding

A

weak electrical between hydrophobic side chains

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13
Q

covalent bonds in folding

A

between sulfhydryl groups disulfide bonds

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14
Q

ionic bonding in folding

A

between groups with full and opposing charges

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15
Q

dimers

A

proteins with 2 polypeptide units

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16
Q

Homodimers

A

2 identical subunits

17
Q

Heterodimers

A

nonidentical subunits

18
Q

Tetramer

A

4 polypeptide chains

19
Q

Prions

A

altered forms of normal proteins

20
Q

Denatured

A

unfolded proteins
can no longer function normally