Lecture 1 Flashcards

Introduction pH and Buffers Protein Structure ( amino acids, 1 structure) (94 cards)

1
Q

Proteins (4):

A

structure, catalysis, motion, signaling

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2
Q

Carbohydrates:

A

Energy
storage of energy

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3
Q

Lipids:

A

Energy, cell membranes

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4
Q

Nucleic acids:

A

genetic information

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5
Q

What holds macromolecules together (5):

A

Covalent bonds
Hydrogen bonds
Van der Waals interactions
Hydrophobic Effect
Ionic Interactions

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6
Q

Covalent bonds are __ while non- covalent bonds are __

A

Covalent bonds are STRONG while non covalent bonds are WEAKER

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7
Q

What is the energy for covalent bonds:

A

355 kJ mol^-/ (85 kcal mol>-1 ) for C-C bond : 1.54 A

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8
Q

what is the energy for non covalent bonds

A

4-20 kJ mol `-1 (1-5 kcal mol^1)

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9
Q

Non-covalent interactions occur between:

A

Fully charged atoms or molecules

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10
Q

Electrostatic interactions are also called:

A

ionic interactions

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11
Q

What is the equation for electrostatic interactions:

A

E=k ((q1 x q2) / Dr)

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12
Q

Hydrogen bonds occur between :

A

An electronegative atom and a hydrogen covalently bonded to another electronegative atom

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13
Q

Hydrogen bonding vary in bond distance:

A

From 1.5 A to 2.6 A and have bond energies from 4-20 kj mol^-1 (1-5kcal mol^-1)

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14
Q

hydrogen bonds have energies from:

A

4 to 20 kJ mol ^-1 (1-5 kcal mol¨-1)

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15
Q

Hydrogen bonding properties are _ than covalent bonds

A

weaker

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16
Q

Hydrogen bonds are longer than covalent bonds, what is their length:

A

1.5-2.6 A

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17
Q

Van der Waals interactions are based on:

A

transient asymmetry in charge around an atom

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18
Q

van der waals interactions are typically what in energy:

A

2-4 kj mol^-1 (0.5-1kcal/mol)

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19
Q

Van der Waals interactions: Attraction increases as:

A

Two atoms come closer to each other, until they are seperated by the van der Waals distance

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20
Q

Van der Waals interactions: at distances shorter than the Van der Waals contact distance:

A

Strong repulsive forces become dominant

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21
Q

What is the hydrophobic effect?

A

Nonpolar molecules in water can be driven together by the hydrophobic effect:
-It is powered by the increase in entropy of water

-Associated interactions are called hydrophobic interactions

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22
Q

pH is a measure of the H+ concentration and is defined by

A

pH = -log (H+)

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23
Q

The equilibrium constant (K) for the dissociation of water is defined as

A

K = (H+) (OH-) / ( H2O)

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24
Q

KW, the ion constant of water, is defined as

A

Kw = K (H2O) simplified to Kw = (H+) (OH-) = 10^-14

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25
Proton dissociation for a substance HA has an equilibrium constant defined by the expression
Ka = (H+) (A-)/ (HA)
26
The pKa value indicates the susceptibility of proton to removal by reaction with a base:
pka = -log (ka)
27
Henderson-Hasselbalch equation:
pH = pka + log ((A-)/(HA))
28
Weak acids are most effective as buffers at:
pH near the pka value of its acid component
29
What is a buffer?
A solution that can resist pH upon the addition and (small amounts) of strong acid or base
30
What do you need to make a buffer?
A conjugate acid-base pair eg: sodium acetate and acetic acid
31
Over what range is the buffer most effective?
The midpoint
32
What is the central dogma of molecular biology:
DNA -> RNA -> Protein
33
__ are the building blocks of proteins
Amino acids
34
20 proteinogenic amino acids :
An
35
An a-amino acid consists of the a-carbon linked to :
-An amino acid -A carboxylic acid group -A hydrogen atom -A distinctive R group (or side)
36
Chiral amino acids:
- Have four different groups bonded to the a carbon - Exist as two mirror image forms called the L isomer and D isomer
37
zwitterions
an ion carrying both a positive and a negative charge
38
An α-amino acid consists of the α carbon linked to:
– an amino group – a carboxylic acid group – a hydrogen atom – a distinctive R group (or side chain)
39
Chiral amino acids:
-have four different groups bonded to the α carbon. – exist as two mirror-image forms called the L isomer and the D isomer Proteins only contain L isomers
40
pH < pKa :
protonated
41
pH > pKa :
deprotonated
42
Amino acids at neutral pH:
zwitterions
43
The 20 proteinogenic amino acids:
-contain unique side chains that vary in size, shape, charge, hydrogen-bonding capacity, hydrophobic character, and chemical reactivity
44
The 20 proteinogenic amino acids can be placed in one of four groups:
hydrophobic polar positively charged negatively charged
45
Alanine:
Ala A
46
Arginine
Arg R
47
Asparagine
Asn N
48
Aspartic Acid
Asp D
49
Cysteine:
Cys C
50
Glutamine
Gln Q
51
Glutamic Acid
Glu E
52
Glycine
Gly G
53
Histidine
His H
54
Isoleucine
Ile I
55
Leucine
Leu L
56
Lysine
Lys K
57
Methionine:
Met M
58
Phenylalanine
Phe F
59
Proline
Pro P
60
Serine
Ser S
61
Threonine:
Thr T
62
Tryptophan
Trp W
63
Tyrosine
Tyr Y
64
Valine
Val V
65
Asparagine or Aspartic Acid
Asx B
66
Glutamine or Glutamic acid
Glx Z
67
Amino acids: hydrophobic (9)
Glycine (Gly, G) Alanine (Ala, A) Proline (Pro, P) Valine (Val, V) Leucine (Leu, L) Isoleucine (Ile, I) Methionine (Met, M) Tryptophan ( Trp, W) Phenylalanine (Phe, F)
68
Mnemonics to remember the hydrophobic amino acids:
"Gorillas Always Prefer Very Large Islands, Making Wonderful Feasts."**
69
Mnemonics to remember the polar amino acids:
Silly Turtles Yawn Nightly, Quietly Chilling
70
What are the polar amino acids?
Serine (s) Threonine (t) Tyrosine (y) Asparagine (N) Glutamine (Q) Cysteine (C)
71
What are the positively charged amino acids (3)?
Lysine (Lys, K) Arginine (Arg, R) Histidine (His, H)
72
What are the negatively charged amino acids (2)?
Aspartate (Asp, D) Glutamate (Glu, E)
73
ionizable side chain: terminal a - carboxyl group
3.1
74
ionizable side chain: aspartic acid and glutamic acid
4.1
75
ionizable side chain:histidine
6.0
76
ionizable side chain: terminal a-amino group
8.0
77
ionizable side chain: cysteine
8.3
78
Ionizable side chain: tyrosine
10.0
79
ionizable side chain: lysine
10.4
80
ionizable side chain: arginine
12.5
81
The isoelectric point (pI) of a protein is
the pH at which its net charge is zero.
82
aminno acids are linked by __ to form __
amino acids are linked by peptide bonds to form polypeptide chains
82
83
The polypeptide consists of:
– a repeating part called the main chain (or backbone) – a variable part consisting of the distinctive amino acid side chains (R groups)
84
Peptides and primary structure:The backbone has hydrogen-bonding potential:
– Carbonyl (C=O) groups are good hydrogen bond acceptors – NH groups are good hydrogen-bond donors
85
Amino acids joined together by peptide bonds form
peptides
86
Peptide bonds are covalent bonds that are
rigid and planar
87
There are _ rotating bonds around Cα
two
88
primary sequence:Some orientations are more favourable than others due to:
steric hindrance and repulsion.
89
The trans conformation is __ due to __ , the only exception is __
The trans conformation is more favourable (less sterics), the exception is proline
90
amino acids are joined together by peptide bonds that form:
peptides
91
peptide bonds are _ bonds that are _ and _
peptide bonds are COVALENT bonds that are rigid and planar
92
how many rotating bonds are there around ca?
there are two rotating bonds
93
Some orientations are more favorable than others due to:
steric hindrance and repulsion