BIOCHEM lecture 1-10 Flashcards

1
Q

strength between non-covalent interactions

A

permanent dipoles> dipole-induced dipole> London dispersion forces

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2
Q

The water
molecule is non-
linear and

A

carries a
permanent
dipole moment.

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3
Q

The “van der Waals envelope” is the

A

effective “surface of the molecule”.

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4
Q

Two atoms from different molecules rarely come closer together than the sum of

A

their van der Waals
radii

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5
Q

exception to van der waals radii being the closest two atoms can get

A

Hydrogen

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6
Q

unit conversion for vdW radius

A

10 Å = 1 nm = 10 -9 m

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7
Q

when water is ice it

A

interacts tetrahedrally with four other molecules

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8
Q

D-H =

A

weakly acidic “donor” group, such as O-H, N-H

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9
Q

A =

A

weakly basic “acceptor” atom such as O, N

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10
Q

D-H…A

A

hydrogen bond

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11
Q

The permanent dipoles of water molecules interact very favorably with charged ions in
solution,

A

forming a “hydration shell”.

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12
Q

no difference in enthalpy (entropy drive) in a

A

transfer of hydrocarbaons from water to nonpolar solvents

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13
Q

amphiphillic/amphipathic

A

have both polar and non-polar segments

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14
Q

clustering lipids

A

increase the entropy of a system (less rotational restriction)

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15
Q

H-bonding within water facilitates its

A

ionization

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16
Q

H+ should be written as

A

H3O+ technically

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17
Q

1 liter of water there is

A

55.5 moles

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18
Q

Kw[10E-14]=

A

[H+ 10E-07][[OH- 10E-07]

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19
Q

HH equation

A

pH = pKa +log ([base]/[acid])

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20
Q

protons can be used to:

A
  • Induce a large conformational change of a protein.
  • Store energy – as a proton concentration difference
    across a membrane
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21
Q

The pH of fluids surrounding
cells, and of the cytosol inside
the cell, is around 7.

A

However, in the organelles
called endosomes, the pH is
lower. -> used by influenza virus to infect a host cell bc pH differences inducesconformational change in surface protein

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22
Q

protons cannot cross a

A

lipid membrane

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23
Q

periplasm

A

the space between two membrane of bacterial cells

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24
Q

low proton concentration in

A

cytoplasm

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25
high proton concentration in
periplasm
26
serine=ser=s
polar
27
hydrophobicity of side chains
phe>ile>ala
28
proline
makes ring with N in backbone
29
isoleucine
1 of 2 CHIRAL side chaines
30
uncharged + polar
serine
31
uncharged + polar
cycsteine
32
uncharged + polar
threonine
33
uncharged + polar
glutamine
34
uncharged + polar
asparagine
35
aliphatic + nonpolar
glycine
36
aliphatic + nonpolar
alanine
37
aliphatic + nonpolar
proline
38
aliphatic + nonpolar
valine
39
aliphatic + nonpolar
leucine
40
aliphatic + nonpolar
isoleucine
41
aliphatic + nonpolar
methionine
42
Threonine
1 of 2 CHIRAL side chains
43
His
pK of ~ 6 means that at neutral pH the imidazole ring is both in its protonated and unprotonated state; at a pH below the pK a larger fraction is protonated than unprotonated; at pH values above the pK a larger fraction of the side chain is unprotonated than protonated.
44
negatively charged
aspartate (COO-)
45
negatively charged
glutamate (COO-)
46
aspartate and glutamate
* These side chains are very hydrophilic. * The side chain carboxylates are often found in active sites * The carboxylates can coordinate metals – in particular Mg2+ and Ca 2+.
47
aromatic
phenylalanine
48
aromatic
tyrosine
49
aromatic
trytophan
50
alanine
a
51
arginine
R pKa 12.5
52
asparagine
N
53
aspartic acid
D pKa 3.9
54
cycsteine
C pKa 8.3
55
glutamine
A
56
glutamic acid
E pKa 4.2
57
glycine
G
58
Histidine
H pKa 6
59
isoleucine
I
60
leucine
L
61
lysine
K pKa 10
62
methionine
M
63
phenylalanine
F
64
proline
P
65
serine
S
66
threonine
T
67
tryptophan
W
68
tyrosine
Y pKa 10.1
69
Valine
V
70
amino group
-below pka nh3+ -above pka nh2
71
hydroxyl group
-below pka oh -above pka o-
72
SH-group
-below pka sh -above pka s-
73
imidazole
-below pka one positive charge -above pka uncharged
74
the pka of the SAME functional group can be different in
different molecules
75
oxidation of cysteine to cystine
forms disulfide bonds
76
non-standard enzymes come from
post-translational modifications
77
protein kinases
attach phosphates
78
O-glycosylation
The oligosaccharide is attached to side chain O of a Ser or Thr
79
N-glycosylation
The oligosaccharide is attached to side chain N of an Asn
80
core protein
pentasaccharide “core in protein glycosylation
81
antenna protein
Such complex antennas are very specific markers of proteins on a cell surface.
82
protein glycosylation
addition of suagrs onto aa side chains
83
pka of N-terminal NH3+
8
84
pka of C-terminal COO-
4
85
if one peptide unit is fixed phi and psi define
orientation of second peptide unit
86
course of a polypeptide chain is defined by a
pair of dihedral angles (phi and psi) per aa residue