L1-2: The Building Blocks of Life Flashcards

(32 cards)

1
Q

What are the 20-22 amino acids?

A

Alanine, Asparagine, Arginine, Aspartic acid, Cysteine, Glycine, Glutamine, Glutamic acid, Histidine, Hydroxyproline, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Proline, Selenocysteine, Serine, Tryptophan, Tyrosine, Threonine, Valine

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2
Q

Which amino acids are charged?

A

-ive
Aspartic acid
Glutamic acid
+ive
Arginine
Histidine
Lysine

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3
Q

Which amino acids not directly encoded?

A

Selenocysteine and Hydroxyproline

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4
Q

What amount of a human is protein (dry weight %and wet weight kg)

A

~25% and 12kg wet

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5
Q

What is the approximate number of proteins in the human body?

A

20,000

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6
Q

What are the 4 levels of protein structure?

A

primary, secondary, tertiary and quaternary

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7
Q

What 2 structures are formed from secondary protein structure?

A

alpha helix and beta pleated sheet

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8
Q

What is the bond between amino acids called?

A

Peptide bond

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9
Q

What are the 2 classifications of amino acids?

A

L and D amino acids

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10
Q

How is the ribosome structured?

A

It has large and small sub-units

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11
Q

What would be stopped when protein synthesis is a drug target? And where would the target be?

A

Peptide bond formation and at the active site of the ribosome

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12
Q

Which type of amino acids do ribosomes make?

A

L-amino acids

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13
Q

Why are the bonds in a tetrahedral arrangement in amino acids?

A

To minimize overlap

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14
Q

What arrangement do electron shells adopt in proteins?

A

sp3 hybridization which is in a tetrahedron

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15
Q

What does it mean when a carbon is chiral?

A

The different chiral forms of a molecule cannot be superimposed on each other

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16
Q

How can you detect 2 different chiral molecules and what are they called?

A

Use plane-polarized light from a polarizer which rotates clockwise or anticlockwise and they are called enantiomers

17
Q

What is L/D configuration relative to?

A

D-glyceraldehyde

18
Q

What handed are alpha helicies?

19
Q

What is an example of a drug used that changed enantiomers in the body?

A

Thalidomide (late 1950s)

20
Q

What are the amino acids with hydrophobic side chains?

A

Ala, Val, Ile, Leu, Met, Phe, Tyr, Trp

21
Q

What is each amino acid in a sequence called?

22
Q

What are the characteristics of the peptide bond?

A

Rigid and planar

23
Q

What is electronegativity?

A

Attraction of different elements for electrons due to atomic number and distance from nucleus of valence electrons

24
Q

What are the slight charges of the amide and carbonyl groups?

A

Amide- positive
Carbonyl- negative

25
Why are hydrogen bonds important?
Secondary structure arises from backbone hydrogen bonding and higher level structure has large hydrogen bonding contribution
26
how many residues per turn are there in a 100 degree repeat?
3.6
27
What amino acids are preferred in alpha helices?
Ala, Glu, Leu, Met, Ile, Lys, Phe, Trp
28
On average, how many residues do alpha helices contain?
11
29
How many residue repeats do beta strands have?
2
30
What are the preferred amino acids in beta strands?
Ile, Tyr and Val
31
What type of handedness do beta pleated sheets usually have?
Right-handed twist
32
What do beta-sheets often form?
The core of globular proteins