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GMC > Lecture 17&18- proteins and amino acids > Flashcards

Lecture 17&18- proteins and amino acids Flashcards

1
Q

The biological world stages

A

Biosphere -> domains of life + viruses -> phylum, genus, species, strain -> cells -> molecular biology

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2
Q

It is suggested that …. evolved through ….

A

Eukaryotes
Archea

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3
Q

Alanine

A

ALA
A

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4
Q

Arginine

A

Arg
R

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5
Q

Asparagine

A

Asn
N

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6
Q

Aspartic acid

A

Asp
D

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7
Q

Cysteine

A

Cis
C

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8
Q

Glutamic acid

A

Glu
E

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9
Q

Glycine

A

Gly
G

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10
Q

Histidine

A

His
H

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11
Q

Isoleucine

A

Ile
I

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12
Q

Leucine

A

Leu
L

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13
Q

Lysine

A

Lys
K

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14
Q

Methionine

A

Met
M

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15
Q

Phenylalanine

A

Phe
F

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16
Q

Proline

A

Pro
P

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17
Q

Serine

A

Ser
S

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18
Q

Threonine

A

Thr
T

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19
Q

Tryptophan

A

Trp
W

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20
Q

Tyrosine

A

Tyr
Y

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21
Q

Valine

A

Val
V

22
Q

In vertebrates, … of the 20 amino acids can be made in cells and … cannot be synthesised in human cells

A

11
9

23
Q

All amino acids except … have the same structure:
-….. carbon atom (chiral in all amino acids except glycine
-…… group
-….. group
-…… group

A

Alpha
Carboxyl
Amine
R

24
Q

Chirality/ handedness

A

The object or molecule can’t be superimposed on it’s mirror image by any translations or rotations

25
Q

Amino acids are always ….-isomers

A

L

26
Q

Aliphatic

A

R-group chain isn’t branched

27
Q

Aromatic

A

R-group os based on a benzene ring (hydrophobic)

28
Q

Polar

A

The R-group carries a small charge, both positive and negative

29
Q

Charged

A

The R-group is ionisable creating positive or negative charge depending on pH and type of R group

30
Q

In ….. amino acids have two ionisable groups: ….. and …..

A

Solution
Carboxyl
Amine

31
Q

Amphoteric

A

An acid can both donate and accept protons

32
Q

pKa

A

Acid dissociation constant
measure of how easily the proton is lost
How well something mops up protons
As dissociation increases, pKA decreases
Low pKa = strongly acidic

33
Q

….. & … have delocalised charge

A

Arg
His

34
Q

…. & …. are polar- form H-bonds

A

Ser
Thr

35
Q

Zwitterion

A

An ion that contains 2 functional groups, 1 +ve and 1 -ve

36
Q

Hydropathy values

A

How well a protein mixes with water
High value= hydrophobic

37
Q

AA with aromatic R groups

A

Phe, Tyr, Trp

38
Q

AA with small R-groups

A

Gly, Ala

39
Q

AA with kinks

A

Pro

40
Q

AA with thiol group

A

Cys

41
Q

Electrostatic/ ionic interactions

A

Occur between oppositely charged atoms
Strongest as ionic bonds formed between fully/ formally charged atoms

42
Q

Proteins with R-groups with charged atoms for ionic bonds

A

Asp, Glu, Lys, Arg, His

43
Q

Example of essential ionic bond in enzyme activity

A

ATPase
ATP -> ADP
ATPase hydrolyses ATP and a phosphate group is lost
lysine amino acid R-group bonds ionically to ATP

44
Q

Polar bonds: hydrogen bonding

A

Specialised type of polar interaction
Involves slightly electropositive H atom and an electronegative acceptor atom
Mostly form between H, O & N

45
Q

Salvation shell

A

Formed by water around proteins
Formed by a network of hydrogen bonds

46
Q

Van der Waals interactions

A

Temporary dipole formed
Can induce a dipole on adjacent atoms

47
Q

Hydrophobic forces

A

Not bonds
Hydrophobic molecules crowd together in water
Allows hydrophobic packing

48
Q

AA that are hydrophobic

A

Val, Leu, Ile, Met

49
Q

hydrophobic AA stick together in….

A

Cores

50
Q

Hydrophobic forces Increase with increasing …. and …..

A

Temperature
Salt

GMC (25 decks)

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