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LS 3 Key Terms > [Lec 3] Key Terms: Structure of Proteins > Flashcards

[Lec 3] Key Terms: Structure of Proteins Flashcards

1
Q

Glycine

A

Gly, G; 1. neutral non-polar; 2. smallest amino acid, most flexible

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2
Q

Alanine

A

Ala, A; neutral non-polar

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3
Q

Valine

A

Val, V; neutral non-polar

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4
Q

Isoleucine

A

Ile, I; neutral non-polar

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5
Q

Tryptophan

A

Trp, W; neutral non-polar

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6
Q

Phenylalanine

A

Phe, F; neutral non-polar

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7
Q

Proline

A

Pro, P; 1. neutral non-polar; 2. covalent bond with amino group restricts conformational group, DISRUPTS ALPHA HELIX FORMATION

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8
Q

Methionine

A

Met, M; neutral non-polar

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9
Q

Leucine

A

Leu, L; neutral non-polar

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10
Q

Aspartic Acid

A

Asp, D; acidic

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11
Q

Glutamic Acid

A

Glu, E; acidic

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12
Q

Lysine

A

Lys, K; basic

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13
Q

Arginine

A

Arg, R; basic

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14
Q

Histidine

A

His, H; basic

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15
Q

Serine

A

Ser, S; neutral polar

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16
Q

Threonine

A

Thr,T; neutral polar

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17
Q

Cysteine

A

Cys, C; 1. neutral polar; 2. two cysteine resides can form a disulfide bond

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18
Q

Tyrosine

A

Tyr, Y; 1. neutral polar; 2. contain both hydrophobic ring and -OH group; 3. sometimes known as aromatic of neutral polar

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19
Q

Asparagine

A

Asn, N; neutral polar

20
Q

Glutamine

A

Gln, Q; neutral polar

21
Q

neutral non-polar

A

hydrophobic, inside lipid bilayer; in R, all contains methyl group, aromatic rings, or hydrogen alone. None are very electronegative so hydrogen bonds don’t form

22
Q

neutral polar

A

hydrophillic, outside lipid bilayer; in R, all contain electronegative oxygen or sulfur atoms which form hydrogen bond with molecules like water

23
Q

acidic

A

negative charge and contains an oxygen

24
Q

basic

A

positive charge and contains a nitrogen

25
Q

Alpha Helix

A

secondary structure; right handed helix; 1. 3.6 residues/turn; 2. H-bond between every 4th amino acid on backbone; 3. forms a rigid structure; 4. R-groups project out from helix ; 5. H-bonds are parallel to axis of helix; 6. side chains interact to hold two alpha helices together in coiled coil

26
Q

Leucine Zipper

A

motif; very stable; leucine in every 4th amino acid; alpha helix

27
Q

Beta-Pleated Sheets

A

secondary structure; 1. planar peptide bonds with bend at Carbon; 2. H-bonding between one beta strand and another between backbone; 3. R-groups alternate above and below sheet; 4. found parallel and antiparallel

28
Q

Tertiary Structure

A
  1. folded structure of the entire polypeptide chain; 2. determined largely by primary structure
29
Q

Anifinsen Experiment

A

Showed that protein can fold correctly by itself. Primary structure is sufficient to produce correct tertiary structure

30
Q

chaperone proteins

A

help larger proteins fold properly

31
Q

motifs

A

important features smaller than domains

32
Q

structural motif

A
  1. independently folding region; 2. continuous sequence of amino acids; 3. multiple domains possible
33
Q

functional domain

A
  1. region or domain required for specific function; 2. structure of protein may not be known; 3. functional domain may be part of a larger structural domain or be made up of several smaller structural domains
34
Q

quaternary structure

A

arrangement of multiple subunits into larger complex

35
Q

subunits

A

each polypeptide of a multimeric unit; 1. often held together by non-covalent bonds, but disulfide bonds may form between subunits too; 2. multimeric proteins can be made up of identical (homo) or different (hetero) subunits

36
Q

subunit structure of a protein

A

the number and relative position of the subunits in multimeric proteins

37
Q

protein enzymes

A

catalyzes a chemical reaction

38
Q

Zinc finger motif

A

recognizes specific DNA sequences

39
Q

specificity

A

DNA binding can be “specific” (nucleotide sequence matters) or “nonspecific” (nucleotide sequence doesn’t matter)

40
Q

affinity

A

how well proteins bind (higher affinity=tighter binding)

41
Q

competitive inhibitor

A

binds the active site

42
Q

allosteric inhibitor

A

changes active site by binding somewhere else

43
Q

Glycosylation

A

addition of sugar molecule; added to Asn, Ser, or Thr; can affect protein stability, conformation, and/or function

44
Q

Phosphorylation

A

addition of phosphate; added to Ser, Thr, Tyr; can affect protein stability, conformation, and/or function

45
Q

Acetylation

A

addition of acetyl group; added to many residue and backbone of N-terminus; can affect protein stability, conformation, and/or function

46
Q

Methylation

A

addition of a methyl group; added to Lys and Arg; can affect protein stability, conformation, and/or function

LS 3 Key Terms (8 decks)

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