Biochemistry - First Half Flashcards

Eat up the midterm and exam (55 cards)

1
Q

Non-Polar Amino Acids

A

A, V, I, L M, F

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2
Q

Moderately Non-Polar AA

A

Y, W, C, G, P

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3
Q

Polar AA

A

S, T, N, Q

Aparagine, Glutamine

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4
Q

Positive AA

A

H, R, K

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5
Q

Negative AA

A

D,E
Aspartate, Glutamate

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6
Q

AA that can accept or donate H+ from their sidechains

A

S, T, C, Y, D, E

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7
Q

AA with Ionizable Side Chains

A

D, E, Y, C, R, H, K
- positives
- negatives
- and cysteine and tyrosine

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8
Q

Partition CT

A
  • Silica gel (polar)
  • np out first
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9
Q

Thin Layer CT

A
  • in lab
  • ninhydrin
  • silica gel
  • np go further
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10
Q

Ion Exchange CT

A

Cation - bind +
Anion - bind -
change pH or outcompete

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11
Q

Affinity CT

A

Ligand attach to beads in column
- prots bind to ligand
- add salt to weaken bond to ligand
- can add a tag to bind the ligand with more specificity

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12
Q

Immobilized Metal CT

A
  • Ni2+ resin
  • cluster of His bind tightly
  • change prot structure
  • add imidazole to elude
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13
Q

Gel Filtration CT

A
  • size
  • polymeric gels
  • large out first
  • antilog of y axis to find molar mass
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14
Q

Electrophoresis

A

size shape charge
- use electric field to differ based off charge
- speed depends on size
- uses polyacrylamide gel
- visualize with Coomassie blue

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15
Q

Isoelectric Focusing

A

pH gradient
- stops where isoelectric point = 0

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16
Q

SDS - electrophoresis

A
  • partially unfolds
  • large negative charge
  • uniform charge per unit size
  • based on weight
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17
Q

2D gels

A
  • separate by isoelectric point then weight
  • SDS-PAGE and isoelectric focusing
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18
Q

Mass Spectrometry

A
  • vaporize with lazar
  • charged particles to detector
  • faster = smaller
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19
Q

Sanger Method

A

Fluorodinitrobenzene
- reacts with Nterm - NH2 is nucleophile (basic)
- - attacks at C-F which is electrophile
- HF as leaving agents
- destroys rest of chain (because acid hydrolysis breaks all peptide bonds)
- Nterm with Dinitrobenzene is yellow so easily found

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20
Q

Edman degradation

A

a) coupling with PITC - done in basic conditions so NH2 is deprotonated and can act as a nucleophile
b) cyclization - so acts as an acid a protonates - causing cyclization
- increases strength of S bond (nucleophile) and cycles up to C=O
- - breaking bond to next NH to restart

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21
Q

trypsin

A
  • Arg, Lys
  • not with proline to the right
  • always cterm is Lys and Arg
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22
Q

chemotrypsin

A
  • Phe, Trp, Try
  • not with proline
  • on right side
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23
Q

cyanogen bromide

A
  • Met
  • yes with proline
  • converts Met to Homocystein (Hse)
24
Q

Linus Pauling

A
  • peptide bond has double bond character
  • CN is planar and cannot rotate
  • can rotate at C-C so planes can rotate
25
Helical
- 3.6 aa per turn - 5.4 A long each turn - Carboxylate of 1 lines up with Amide of 5
26
Beta
- space for bulky side chains - WYF needs VIT C
27
Urea
- weakens the hydrophobic effect - denaturing agent
28
2-mercaptoethanol
- converts disulfide bonds back to their regular seperate cystein groups - disulfide reducing agent
29
Common FA
- unbranched - even number of carbons - cis bonds - methylene bridged
30
Let my pal stay around
Laurate 12 Myristate 14 Palmitate 16 Stearate 18 Arachidate 20
31
Phosphate head group
Phosphatidic Acid - just an H -2 or about -1.5 (resonance) Choline - 0 Ethanolamine - 0 Serine - (-1) Glycerol - (-1)
32
Absorption Chromatography
- neutral eludes first - then polar - then charged
33
Analysis of FA
Transesterification to FA methyl esters (volatile) - seperated based on size and degree of unsat - mass spec - FAME can be used in gas-liquid chromatography or high performance liquid chromatography
34
Enantiomers
Differ at ALL chiral carbons - identical chem properties
35
Diastereomers
Differ at more than 1 chiral C - not identical chem properties
36
Epimers
A diastereomer that differs at ONLY 1 chiral C
37
Chiral Carbons of Aldoses vs Ketoses
- ketoses - have isomers chiral carbons with same C amount - aldoses have more b/c they are on the end 2^n - n is the number of chiral centers
38
Anomers
Differ in orientation at the anomeric carbon
39
Glycoside
- a sugar component bonded to a non-sugar component via a glycosidic linkage
40
A-T
- 2 H bonds
41
G-C
- 3 H bonds
42
DNA
- antiparallel - right handed - major minor groove - bases 3.4 A apart - one turn 10A Major Groove - more accessible to interactions w proteins that recognize a specific DNA sequence
43
ATP to ADP and Pi
1) releases electrostatic repulsion 2) Pi has more resonance stability than ATP - further releasing PPi to 2 Pi releases more electrostatic repulsion
44
CoA
comes from pantothenic acid (B5) - carriers acids (acyl groups)
45
Acetyl CoA
is acetone with a CoA
46
NAD+ and NADP+
from Niacin (B3) - accept hydride ion H- - redox at nicotinamide ring
47
FAD and FNM
from vitamin riboflavin (B2) - prosthetic groups - accept 1 or 2 H atoms - can form a semiquinone radical
48
Rotenone
inhibits C1
49
barbiturates
inhibits C1
50
antimycin A
inhibits C3
51
CN- or CO
inhibits C4
52
Add ADP and Pi
increases ATP synthase
53
Add succinate
increases ETC
54
Venturicidin or Oligomycin
inhibit ATP synthase
55