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Biochemistry > Amino Acids and Proteins > Flashcards

Amino Acids and Proteins Flashcards

1
Q

What determines 3D structure and biological properties of proteins?

A

The sequence of the AA that are linked together

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2
Q

D or L type proteins are found naturally in humans?

A

its L-type (but we can metabolize D, just cant incorporate)

D type is the sugars we can handle

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3
Q

Acidic AAs

A

Aspartic Acid

Glutamic Acid

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4
Q

Basic AAs

A

Lysine

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5
Q

Non-polar AAs

A

Glycine, Leucine, Alanine, Phenylalanine

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6
Q

neutral AAs

A

Serine, Cysteine, Threonine, Tyrosine

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7
Q

Asn

Asp

Gln

Glu

A

Asparagine

Aspartate

Glutamine

Glutamate

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8
Q

Tell me about the formation of cystine

A

2 cysteines can spontaneously oxidize to form cystine (the sulfurs bond to each other)

*cystinuria - the transport protein that reabsorbs Arg/Lys/CYSTINE is busted. so cystine cant be reabsorbed and shows up in the urine! (Arg/Lys are soluble)

can have kidney stones (made of cystine)

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9
Q

Primary structure

Secondary structure

A

sequence of AA

alpha helix or beta pleated sheets (hydrogen bonding)

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10
Q

keratin

hard vs. soft keratins

A

major component of external protective layers in mammal

  • hard have a high sulfur content (nails, horns, beak)
  • soft (wool, fur, skin)
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11
Q

Hair cell?

A 
alpha helices
3 alpha helixes = 1 protfibril
11 protofibrils = 1 microfibril
100s of microfibrils = 1 macrofibril
many macrofibrils = one hair cell
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12
Q

collagen

A

major protein component of connective

forms insoluble fibers of great strength

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13
Q

collagen structure

A

without vitamin C (a cofactor) there can be no hydroxylation of proline/lysine and the necessary bonds between chains cannot form (post-translational modification) that produces collagen

no vitamin C = lack of collagen = scurvy

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14
Q

Tertiary structure

A

3D structure
proteins fold during and after synthesis (polar groups on surface, non-polar AAs in the interior - drives the folding pattern)

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15
Q

molecular chaperons?

A

example = heat shock proteins - salvage the denatured protein or break it down if its too far gone

chaperons* - job is actually to delay folding - prevents misfolding, its faster/more efficient

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16
Q

Prion diseases

A

degeneration of brain tissue caused by conversion of normal protein to misfolded protein

introduction of this misfolded protein by infection, ingestion, or mutation is bad news

  • genetic: CDJ (humans), BSE (cows), Scrapie (sheep)
  • infection transmitted via pig human growth hormone injection (not relevant today because we use bacteria to synthesize hormones)
17
Q

Quaternary structure

A

example = hemoglobin (interaction of 4 myoglobin subunits, each with one site for Oxygen binding)

18
Q

cooperative binding of oxygen (Hb)

A

once one Hb subunit binds oxygen the other 3 change confirmation to relaxed state and are more likely to bind oxygen

19
Q

Bohr effect

A

Hydrogen ions (and CO2) promote the release of oxygen

source of H+: lactic acid from active muscle tissue

  • BPG stabilizes deoxyhemoglobin
  • binding of BPG promotes release of oxygen (to tissues that need oxygen most)

Fetal Hb cant bind BPG and therefore has an enhanced affinity for oxygen

20
Q

Sickle cell

A

genetic disease - point mutation - cause

  • RIGID SICKLE SHAPE - deoxy Hb polymerizes
  • ANEMIA (sickle cells more readily broken down) - also because of this billirubin, a breakdown product of RBCs cant be excreted fast enough and accumulates causing gallbladder stones
  • ISCHEMIA (their shape causes blockages in blood vessels
21
Q

What does it mean to denature a protein?

A

break apart 3D structure (primary structure remains)

extremes of ph or temperature, organic solvents, radiation

22
Q

What is a conjugated protein?

A

a protein with a non-protein component attached

lipoproteins (HDL)
glycoproteins (collagen, FSH, TSH)
nucleoproteins (histomes)

23
Q

Remember this key fact

A

Information for folding is contained in the sequence of the amino acid

Biochemistry (15 decks)

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