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Amino Acids > Properties > Flashcards

Properties Flashcards

1
Q

Which amino acids are hydrophobic and aliphatic?

A

Glycine (G), Alanine (A), Leucine (L), Valine (V), Isoleucine (I), Methionine (M), Proline (P)

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2
Q

Which amino acids are hydrophobic and charged?

A

Phenylalanine (F) and Tryptophan (W)

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3
Q

Which amino acids are hydrophilic and charged?

A

Aspartate (D), Glutamate (E), Lysine (K), Histidine (H), Arginine (R)

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4
Q

Which amino acids are hydrophilic and neutral?

A

Asparagine (N), Glutamine (Q), Serine (S), Threonine (T), Cysteine (C)

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5
Q

What is the first amino acid in a protein sequence?

A

Methionine

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6
Q

Which amino acid with a sulfide R group creates peptide bonds?

A

Cysteine

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7
Q

What do tryptophan, tyrosine, and phenylalanine have in common?

A

Absorb light at 280 nm, are aromatic

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8
Q

How are serine and threonine modified?

A

OH glycosylation and phosphorylation

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9
Q

How is asparagine modified?

A

N-liked glycolsylation

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10
Q

How is proline modified and how does it affect the structure of DNA?

A

Can be hydroxylated, ring causes bend in DNA structure

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11
Q

What is unique about a dipeptide bond?

A

Stronger than a normal bond but with double bond characteristics (Such as rotational freedom)

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12
Q

After how many amino acids is a polypeptide considered a protein?

A

50

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13
Q

What is common to all peptide chains?

A

N terminal, C terminal, moves from N to C terminal

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14
Q

What is the range of amino acids in a naturally occurring protein?

A

50-2,000

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15
Q

What type of interaction is present in a primary protein structure?

A

Peptide bonds

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16
Q

Which interactions are present in a secondary protein structure?

A

Peptide bonds and hydrogen bonds

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17
Q

Name the types of secondary protein structure and the characteristics for each type.

A

Alpha helix: Rod-like structure, coiled peptide chain, R groups stick out of helix, bonding is parallel to the chain (In line with the helix), 3.6 AAs per turn, naturally occur in right handed helices

Beta sheet: Extended polypeptide chain, H bonding between different polypeptides, strands can run in parallel or anti-parallel (With beta turns), often contain proline because it is bulky

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18
Q

How is a protein stabilized in the tertiary structure?

A

Weak, non-covalent bonds between R-groups

19
Q

What types of interactions can be found in a tertiary protein structure?

A

Hydrogen bonding, electrostatic interactions, hydrophobic interactions, Van der Waals forces, disulphide bonding between cysteine residues

20
Q

What is characteristic of a quaternary protein structure?

A

Several polypeptide units interacting, covalent and non-covalent interactions, bonds are able to break and reform repeatedly, allosteric proteins have quaternary structure

21
Q

How can proteins be denatured?

A

Heat (Breaks weak bonding), pH (Disrupts H bonding), detergents/organic solvents (Disrupts hydrophobic bonding), chaotropic agents (Form H bonds with AAs and disrupts existing H bonds)

22
Q

Name three agents that can denature primary and tertiary protein structure.

A

Urea, guanine HCl, mercaptoethanol (Reduces disulphide bonds)

23
Q

What is unique about denaturing a tertiary protein structure?

A

It can be reformed if all information is retained and denaturing agents are removed

24
Q

Which protein stage determines the entire protein structure?

A

Primary

25
Q

What would be affected if the primary structure of a protein was altered?

A

Ligand binding, enzyme activity, protein shape

26
Q

How is the structure of collagen different than a normal protein?

A

Triple helix, 3 AA per turn, 3 collagen strands intertwined, glycine is every third AA due to its size

27
Q

How is the collagen triple helix stabilized?

A

By H bonding between CO, NH, OH

28
Q

How is scurvy caused?

A

A deficiency in Vitamin C causes prolyhydroxylase to remain inactive, meaning proline isn’t hydroxylated and less H bonds are formed. This causes collagen to be unstable.

29
Q

How is osteogenesis imperfecta caused?

A

Glycine mutation, inherited

30
Q

What two classifications can proteins fall under?

A

Globular: A lot of tertiary structures, non-structural, R-group interactions, a lot of alpha helices, ligand binding sites

Fibrous: A lot of beta sheets, mostly secondary structure, a lot of H bonding, structural

31
Q

Describe the protein changes that occur with prion diseases.

A

Proteins change from globular to fibrous which causes an aggregation of protein and disrupts neural outputs.

32
Q

Which codon represents Scrapie resistance and which codon represents Scrapie susceptibility?

A

ARR, VRQ

33
Q

What happens when a ligand binds to a protein with quaternary structure?

A

A comformational change takes place

34
Q

What states can a subunit be in in order to bind a ligand?

A

Tense state (Less likely to bind ligand) or Loose state (Likely to bind ligand)

35
Q

What do positive allosteric regulators do?

A

Increase ligand affinity

36
Q

What do negative allosteric regulators do?

A

Decrease ligand affinity

37
Q

Hemoglobin (Oxygen binding) is regulated by which substances?

A

CO2, H+, oxygen that has bound to one of the active sites

38
Q

What is proteomics?

A

The study of the protein profile of a cell or tissue

39
Q

What is genomics?

A

The study of the genome

40
Q

What is studied in qualitative proteomics?

A

Differences in AA sequence

41
Q

What is studied in quantitative proteomics?

A

Increases or decreases in proteins

42
Q

What does SDS-PAGE accomplish?

A

Separating proteins by size and charge

43
Q

What is isoelectric focusing?

A

Separating proteins by charge only, using pH

44
Q

What is the point at which a protein has no net charge during isoelectric focusing?

A

Isoelectric Point

Amino Acids (1 decks)

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