CHEM Spectroscopy and Separations Flashcards

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1
Q

Infrared Spectroscopy

A

For Functional Groups

Uses radiation w/ a frequency lower than that of visible light to vibrate covalent bonds (must have dipole moment)

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2
Q

1550 - 1650 wavenumber (cm-1)

A

C=N

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3
Q

1600 - 1680 wavenumber (cm-1)

A

C=C

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4
Q

1650 - 1780 wavenumber (cm-1)

~1700

A

C=O

Sharp

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5
Q

2100 - 2260 wavenumber (cm-1)

A

C≡C

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6
Q

2220 - 2260 wavenumber (cm-1)

A

C≡N

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7
Q

3200 - 3600 wavenumber (cm-1)

A

O-H

Broad

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8
Q

3300 - 3500 wavenumber (cm-1)

A

N-H

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9
Q

Area below 1500 wavenumber (cm-1)

A

Fingerprint region

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10
Q

NMR Spectroscropy

Nuclear Magnetic Resonance

A

Characterizes a molecule’s atoms

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11
Q

Left side of NMR

A

Downfield = DEshielded = close to e- withdrawing groups

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12
Q

Right side of NMR

A

Upfield = shielded = far from e- withdrawing groups

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13
Q

1-HNMR (proton NMR) area under peak

A

Corresponds to # of equivalent hydrogens

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14
Q

Splitting

A

N + 1 Rule
Singlet, doublet, triplet, etc.
is determined by # of hydrogens on adjacent atom

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15
Q

0.9 ppm shift

A

-CH3

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16
Q

1.0 - 5.5 ppm shift

A

-CH2OH

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17
Q

2.0 - 3.0 ppm shift

A

-C≡CH

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18
Q

4.5 - 6.0 ppm shift

A

-CH=CH-

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19
Q

6.0 - 8.4 ppm shift

A

Ar (aromatic ring) - H

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20
Q

9.5 ppm shift

A

-CHO

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21
Q

10.5 - 12.0 ppm shift

A

-COOH

22
Q

N+1 rule

A

For splitting patterns of 1-HNMR

Any peak will be split into a number of smaller peaks equal to the number of adjacent hydrogen atoms plus one

23
Q

13-CNMR

A

Most carbon on earth is in 12-C form but 13-C is used because only nuclei with an odd number of proteins have nuclear spin

Ranges from 0 - 200 ppm

Just like 1-HNMR but looking at Carbons

24
Q

UV-Visible Spec

A

Useful o discern presence of conjugated/aromatic species

25
Q

Mass Spec

A

Helps determine molecular weight (m/z peak; mass to charge ratio peak) of organic compounds

26
Q

Distillation

A

Separates liquids based on Boiling Points

27
Q

Simple Distillation

A

used for BPs > 25˚ apart

28
Q

Fractional Distillation

A

used for BPs < 25˚ apart

29
Q

Vacuum Distillation

A

used for very high BPs

used to lower atmospheric pressures in order to lower BPs

30
Q

Extraction

A

Separates liquids based on solubility/acid-base properties

31
Q

Extraction Requires

A

Immiscible aqueous and organic layers in a sparatory funnel

32
Q

Extraction: to send an ACID into aqueous layer…

A

Add base (deprotonate it)

33
Q

Extraction: to send a BASE into aqueous layer..

A

Add acid (protonate it)

34
Q

Chromatogrpahy

A

Involves a mobile phase and a stationary phase with different properties

35
Q

TLC (thin-layer)

A

Rough measure of polarity
Stationary phase = polar silica
Mobile phase = nonpolar solvent
Rf = distance traveled by compound / distance traveled by solvent

36
Q

Forms of Column Chromatography

A

Stationary phase = in column
Different analyts will be eluted out at different times and can be collected in separate containers

Size-exclusion
Cation-exchange
Anion-exchange
Affinity
Gas
HPLC
37
Q

Gas Chromatography (GC)

A

Vaporizes a sample and passes through a column, then measures retention time
Stationary phase = liquid
Mobile phase = gaseous (like He)

38
Q

HPLC (high performance or high pressure liquid chrom)

A

Rapid method of column chromatography
Stationary phase = polar
Mobile phase = nonpolar

39
Q

RP-HPLC (reverse process)

A

Stationary phase = NONpolar

Mobile phase = polar

40
Q

Other seperation techniques

A

Recrystallization

Filtration

41
Q

Paper Chromatography

A

Mobile phase moves up filter paper via capillary action

42
Q

Size-Exclusion Chromatogrpahy

A

Gel beads contain pores and act as molecular sieve that catches up small particles, making them elue more slowly

43
Q

Ion-Exchange Chrom

A

Relies on charge interactions

44
Q

Anion-exchange Chrom

A

Gel contains cations that trap anions

Anions elute last

45
Q

Cation-exchange Chrom

A

Gel contains anions that trap cations

Cations elute last

46
Q

Affinity Chrom

A

More specific interactions

Ex: Antibody-Antigen

47
Q

Electrophoresis

A

A charge is applied across a gel and molecules migrate due to the applied voltages

48
Q

Gel Electrophoresis

A

Also affected by size due to gel filtration properties

49
Q

SDS-PAGE

A

This allows proteins to be separated by mass alone

SDS and anionic detergent that results in an even distribution of charge per unit mass

50
Q

Isoelectric focusing

A

Uses electrophoresis with a pH gradient to separate proteins by the pI (isoelectric point; the pH where a protein has a net zero charge = zwitterion)

51
Q

Western blotting

A

After electrophoresis, an antibody specific to the separated protein of interest is applied and visualized

52
Q

Enzyme-linked Immunosorbent Assay (ELIZA)

A

Specific visualizable detection antibodies are used to find antigens