Basics (Amino Acids, Proteins, Protein Analysis) Flashcards

(69 cards)

1
Q

1 A = ___ m

A

1 Angstrom = 1 x 10-10 m

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2
Q

How big is the radius of an atom on avg?

A

1-2 Angstroms

1-2 x 10-10 m

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3
Q

What is the average size of a protein?

A

150 residues

30-50 Angstroms

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4
Q

Weight of 1 Hydrogen?

A

1 dalton

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5
Q

What is the average weight of an amino acid?

A

110 daltons

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6
Q

What is a covalent bond? How strong are they?

A
  • A covalent bond is a bond in which electrons are shared between 2 atoms.
  • They are strong (> 100 kcal/mol)
  • Bring atoms close together (1-2 Angstroms)
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7
Q

Order of electronegativity for elements found in proteins?

A

O > N > C = S > H

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8
Q

What is electronegativity?

A

Ability of an atom to attract electrons in a chemical bond

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9
Q

What is a hydrogen bond?

A

Bond formed between an H atom in a polar bond such as O-H or N-H and an electronegative atom like O and N.

  • Weak (1-3 kcal/mol)
  • Contribute to protein structure and stability
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10
Q

Equation for pH

A

pH = -log[H+]

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11
Q

Define pKa

A

The pH at which the concentrations of HA and A- are equal

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12
Q

Describe the chemical structure of an amino acid in 2 parts

A
  1. Set of atoms that make up the backbone of the protein chain
  2. side chain atoms that make them unique
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13
Q

Basic structure of an Amino Acid?

A
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14
Q

What are the Nonpolar Amino Acids?

A

Gly, Ala, Val, Leu, Ile, Met, Pro, Phe, Trp

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15
Q

What are the uncharged but polar amino acids?

A

Asn, Gln, Ser, Thr, Tyr, Cys

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16
Q

What are the charged and polar amino acids?

A

Arg, Lys, Glu, Asp, His

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17
Q

What is special about Cysteine?

A
  • Can form covalent bonds (disulfide bonds) between 2 sulfurs
  • Stabilize or constrain proteins
  • Found in extracellular proteins
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18
Q

Which amino acid forms disulfide bonds that stabilize or ocnstrain proteins?

A

Cysteine

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19
Q

What is unique about Glycine?

A
  • Glycine has no side chain
  • Flexible, found in tight turns
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20
Q

What is unique about Proline?

A
  • Side chain bonds to the nitrogen along the peptide backbone and forms a ring structure
  • Rigidifies a protein
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21
Q

Gly

A
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22
Q

Ala

A
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23
Q

Val

A
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24
Q

Ile

A
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25
Leu
26
Phe
27
Tyr
28
Trp
29
Met
30
His
31
Ser
32
Thr
33
Cys
34
Asn
35
Gln
36
Pro
37
Asp
38
Glu
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Lys
40
Arg
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pKa values for Polar and Charged Amino Acids?
* 3.9 = Aspartic Acid (Asp, D) - NEGATIVE * 4.1 = Glutamic Acid (Glu, E) - NEGATIVE * 6.0 = Histidine (His, H) - NEUTRAL * 10.8 = Lysine (Lys, K) - POSITIVE * 12.5 = Arginine (Arg, R) - POSITIVE
42
Amino Acid Abbrebiation: A
Alanine (Ala)
43
Amino Acid Abbrebiation: C
Cysteine (Cys)
44
Amino Acid Abbrebiation: D
Aspartic Acid (Asp)
45
Amino Acid Abbrebiation: E
Glutamic Acid (Glu)
46
Amino Acid Abbrebiation: F
Phenylalanine (Phe)
47
Amino Acid Abbrebiation: G
Glycine (Gly)
48
Amino Acid Abbrebiation: H
Histidine (His)
49
Amino Acid Abbrebiation: I
Isoleucine (Ile)
50
Amino Acid Abbrebiation: K
Lysine (Lys)
51
Amino Acid Abbrebiation: L
Leucine (Leu)
52
Amino Acid Abbrebiation: M
Methionine (Met)
53
Amino Acid Abbrebiation: N
Asparagine (Asn)
54
Amino Acid Abbrebiation: P
Proline (Pro)
55
Amino Acid Abbrebiation: Q
Glutamine (Gln)
56
Amino Acid Abbrebiation: R
Arginine (Arg)
57
Amino Acid Abbrebiation: S
Serine (Ser)
58
Amino Acid Abbrebiation: T
Threonine (Thr)
59
Amino Acid Abbrebiation: V
Valine (Val)
60
Amino Acid Abbrebiation: W
Tryptophan (Trp)
61
Amino Acid Abbrebiation: Y
Tyrosine (Tyr)
62
Abbreviations for 20 AAs?
63
What is a polypeptide? Peptide bond?
Chain formed when amino acids polymerize through elimination of a water molecule. Pepdide bond is the CO-NH linkage.
64
Number of amino acids in a protein?
between 40-4000 Amino Acids | (A few AA residues is called a peptide)
65
Beginning of a polypeptide chain? End?
Beginning: N-terminus End: C-Terminus
66
Condensation of 2 Amino Acids
67
Primary, Secondary, Tertiary, and Quaternary structure of a protein?
1. **Primary** = amino acid sequence 2. **Secondary** = backbone arrangements (α-helices and β-strands) 3. **Tertiary** = 3D structure of chain 4. **Quaternary** = spatial arrangements of multiple polypeptide chains
68
In an α-helix, residues separated by ___ positions form hydrogen bonds between their backbone atoms.
3
69