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Biochemistry > Quiz 1 > Flashcards

Quiz 1 Flashcards

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1
Q

4 Macromolecules of Biology

A
  1. Protein
  2. Lipids
  3. Carbohydrates
  4. Nucleic Acid
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2
Q

5 examples of Biological Small Molecules

A
  1. Metals/Ions
  2. Vitamins
  3. Hormones
  4. Nucleotide Triphosphates
  5. Sterols
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3
Q

Proteins comprise approximately what percentage of a cells dry weight?

A

50

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4
Q

8 different functions of proteins

A
  1. enzymes
  2. carriers of molecules
  3. structural support
  4. movement
  5. hormones
  6. immune protection
  7. specific response to environment (i.e. vision)
  8. Exotic roles
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5
Q

Draw Amino Acid

A

Draw structure

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6
Q

What enantiomer of Amino acids are found in proteins

A

Only L group

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7
Q

What are the three categories that different AAs can be placed into

A
  1. Charged Polar
  2. Neutral Polar
  3. Nonpolar
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8
Q

AAs numbered in which direction

A

N to C from left to right

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9
Q

Glutamic Acid is what character of AA Charged Polar, Neutral Polar, or Nonpolar

A

Charged Polar

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10
Q

Aspartic acid is what character of AA Charged Polar, Neutral Polar, or Nonpolar

A

Charged Polar

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11
Q

Lysine is what character of AA Charged Polar, Neutral Polar, or Nonpolar

A

Charged Polar

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12
Q

Arginine is what character of AA Charged Polar, Neutral Polar, or Nonpolar

A

Charged Polar

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13
Q

Histidine is what character of AA Charged Polar, Neutral Polar, or Nonpolar

A

Charged Polar

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14
Q

At physiological conditions glutamic acid is what charge?

A

Negative

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15
Q

At physiological conditions aspartic acid is what charge?

A

Negative

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16
Q

At physiological conditions lysine is what charge?

A

Positive

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17
Q

At physiological conditions arginine is what charge?

A

Positive

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18
Q

At physiological conditions histidine is what charge?

A

Positive

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19
Q

Glutamine is what character of AA Charged Polar, Neutral Polar, or Nonpolar

A

Neutral Polar

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20
Q

Aspargine is what character of AA Charged Polar, Neutral Polar, or Nonpolar

A

Neutral Polar

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21
Q

Serine is is what character of AA Charged Polar, Neutral Polar, or Nonpolar

A

Neutral Polar

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22
Q

Threonine is what character of AA Charged Polar, Neutral Polar, or Nonpolar

A

Neutral Polar

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23
Q

Tyrosine is what character of AA Charged Polar, Neutral Polar, or Nonpolar

A

Neutral Polar

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24
Q

Cysteine is what character of AA Charged Polar, Neutral Polar, or Nonpolar

A

Neutral Polar

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25
Valine is what character of AA Charged Polar, Neutral Polar, or Nonpolar
Nonpolar
26
Leucine is what character of AA Charged Polar, Neutral Polar, or Nonpolar
Non polar
27
Isoleucine is what character of AA Charged Polar, Neutral Polar, or Nonpolar
Non polar
28
Methionine is is what character of AA Charged Polar, Neutral Polar, or Nonpolar
Non polar
29
Phenylalanine is is what character of AA Charged Polar, Neutral Polar, or Nonpolar
Non polar
30
Tryptophan is is what character of AA Charged Polar, Neutral Polar, or Nonpolar
Non Polar
31
Proline is what character of AA Charged Polar, Neutral Polar, or Nonpolar
Non Polar
32
Glycine is what character of AA Charged Polar, Neutral Polar, or Nonpolar
Non polar
33
Alanine is is what character of AA Charged Polar, Neutral Polar, or Nonpolar
Non polar
34
In sickle cell which AAs changed
Beta Subunit AA 6 is changed from Glutamic acid to Valine
35
For phosphorylation 1. What is added 2. What kind of Protein is usually modified 3. What is the general effect
1. Phosphate PO4-(2-) 2. Kinases 3. Adding large negative charge causes dramatic effect on protein structure and interaction
36
What classes of AA usually gets modified
Polar or charged
37
Acetylation 1. What is added 2. What kind of Protein is usually modified 3. What is the general effect
1. COCH3 2. Histones 3. Converts +1 to 0 and this makes the protein a target for binding at other proteins
38
Methylation 1. What is added 2. What kind of Protein is usually modified 3. What is the general effect
1. CH3 2. Histones 3. Target for binding by other proteins
39
Glycosylation 1. What is added 2. What kind of Protein is usually modified 3. What is the general effect
1. Sugars 2. Cell surface proteins 3. Stabilizes and adds additional functionality
40
Prenylation 1. What is added 2. What kind of Protein is usually modified 3. What is the general effect
1. Long chain hydrocarbon 2. growth Factors (RAs) 3. Target protein to membrane
41
Ubiquitylation 1. What is added 2. What kind of Protein is usually modified 3. What is the general effect
1. 76 residue polypeptide 2. Cyclin 3. Degradation
42
7 kinds of Protein modification
1. Phosphorylation 2. acetylation 3. Methylation 4. Glycosylation 5. Prenylation 6. Ubiquitylation 7. Disulfide bond
43
Lysine can undergo which kinds of modifications
1. Acetylation 2. Methylation 3. Ubiquination
44
arginine can undergo which kinds of modifications
Methylation
45
Histidine can undergo which kinds of modifications
none
46
Serine and Threonin can undergo which kinds of modifications
1. Phosphorylation 2. O Glycosylation 3. Phosphorylation
47
Tyrosine can undergo which kinds of modifications
Phosphorylation
48
Asparagine can undergo which kinds of modifications
N-Glycosylation
49
Glutamine can undergo which kinds of modifications
none
50
Cysteine can undergo which kinds of modifications
1. Disulfide Bonds 2. Prenylation 3. ubiquitylation
51
Henderson Hasselbach
pH=pKa+log ([A-]/[HA])
52
Henderson Hasselbach the way Myers likes to see it
[A-]/[HA]= 10^ (pH-pKa)
53
If Ph is less than pKa protonation of deprotonation
Protonation
54
If pH is greater than pKa protonation or deprotonation
deprotonation
55
if PI
negative
56
if PI >PH then polypeptide has what kind of charge
positive
57
What can happen to a protein if it is at its isoelectric point
It can precipitate out
58
Free energy equation
dG=dH-TdS
59
What is the balance between free energy and protein folding
balancing delta H from forming attractive/repulsive interactions with the protein becoming more organized when folded.
60
4 types of non-covalent interactions
1. H-BOnds 2. Electrostatic Interactions/Salt Bridges 3. Van Der Waals 4. Hydrophobic
61
what's relationship between H Bonds and strucutre
H bonds have to be linear and that offers a lot of specificity
62
T/F Hydrogen bonds within offer a lot of enthalpy to protein folding
False, hydrophilic AAs can also interact with water/form more H bond with water
63
Electrostatic confer a lot/ a little bit of specificity
A little bit
64
3 Mechanisms to Regulate Protein structure/function
1. Allosteric Control 2. covalent post-translational modifications 3. Proteolytic Cleavage

Biochemistry (5 decks)

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