Mass Analyzers

Árpád Somogyi
Department of Chemistry
University of Arizona

Summer Workshop

Want to do MS or MS/MS ???

Need a Mass Spectrometer

Ionization Mass Detector

source analyzer

inlet all ions sorted

Data
ions
system

1
Moving ions from source to analyzer, etc:

Ions are convenient; they can be

detected efficiently w/ high amplification

accelerate into surface that ejects electrons

controlled with electric and magnetic fields

basis for mass analyzers

numerous design options

Components to move ions

Move ions between ion source and analyzers with
metal plates (electrodes, lenses) to which
potential is applied

Shape and restrict ion beams with series of

electrodes and physical slits

Good ion transmittance efficiency is crucial for

good sensitivity

2
Kinetic energy

E = zeV = qV = ½ mv2

E = kinetic energy
m = mass
v = velocity
e = electronic charge (1.60217e-19 C)
z = nominal charge
V = accelerating voltage

Learning Check

Consider two electrodes,

one at 1000 V and one at ground (0 V)

1000 V 0V

+ ion will travel with kinetic energy of ___________

3
Why do we need mass analyzers?
• To separate ions with a desired
resolution/resolving power.
• Resolving power: the ability of a mass
spectrometer to separate ions with
different mass to charge (m/z) ratios.

FTICR: ultrahigh resolution

J. Throck Watson
“Introduction to Mass Spectrometry” p. 103

4
 Resolution is defined at 10 % valley
M

R=M/∆M

∆M

Let’s talk about mass

analyzers

• Common features
– Accelerated charge species interact with
• Electrostatic (ESA, OT)
• Magnetic (B, ICR)
• Electromagnetic (rf) fields (Q, IT, LT, OT)
– Or just fly (TOF)

5
Desirable characteristics of mass analyzers
(also useful for MS/MS)

1) sort ions by m/z

2) good transmission (improves sensitivity)

3) appropriate resolution (for selectivity)

4) appropriate upper m/z limit

5) compatible with source output

(pulsed or continuous)

For each of the following applications, choose the most

appropriate mass analyzer from the following list. Use each
analyzer only once.

double-focusing sector (BE or EB) quadrupole (Q)

time-of-flight (TOF) FTICR

Analyzer Purpose
______ synthetic organic chemist wants exact mass of
compound
_______ biochemist wants protein molecular weight of
relatively large protein (MW 300,000)
_______ EPA (Environmental Protection Agency) wants
confirmation of benzene in extracts from 3000
soil samples
_______ Petroleum chemist wants to confirm the
presence of 55 unique compounds at one
nominal mass/charge value in a mass spectrum

6
 m/z values are determined by measuring different physical
parameters

Calibration relates the m/z to those physical parameters

Type of analyzer Basis for separation

• electric sector • kinetic energy/z
• magnetic sector • momentum/z
• quadrupole, ion trap • m/z
• time-of-flight • flight time
• FT-ion cyclotron resonance • m/z (resonance frequencies)

Mass Analyzers
• Magnetic (B) and/or Electrostatic (E) (HISTORIC/OLDEST)

• Time-of-flight (TOF)

• Quadrupole (Q)

• Quadrupole Ion Trap (IT)

• Linear Ion Trap (LT)

• Fourier Transform-Ion Cyclotron Resonance (ICR)

Performance Advantages / Disadvantages / $$$

7
 Notice: accelerating voltages vary with analyzer
(has consequences for MS/MS)

• High voltage (keV energy range)

– magnet (B)
– electrostatic (E)
– time-of-flight (TOF)

• Low voltage (eV energy range)

– quadrupole (Q)
– ion trap (IT, LT)
– ion cyclotron resonance (ICR)

Analyzers
Quadrupole
TOF

Quadrupole Ion trap

FTICR
Magnetic sector

8
 Ionization Analysis

MS:

Collide with
target to produce
fragments

MS/MS:

Ionization Selection Activation Analysis

http://www.iupac.org/goldbook/T06250.pdf

9
 Current MS/MS 2008
Tandem in Space
QqQ
Q Trap
Q TOF
TOF TOF
sector
Tandem in Time
Ion Trap (2 or 3 D)
FT-ICR
Trap FT

Analyzers: TOF
Quadrupole
TOF

Quadrupole Ion trap

FTICR
Magnetic sector

10
S im p le s t a n a ly z e r

T im e -o f -flig h t

v = d /t E = zeV = ½ m v2

s o c a n r e la t e flig h t t im e t o m a s s /c h a r g e : _ _ __ _ _ __ _ __

TOF
D
Detector

m/z

V KE = zeV = ½mv2 m = mass

V = velocity
v = D/t D = distance of flight
t = time of flight
½m(D/t)2 = zeV KE = kinetic energy
e = charge
1/ 2
t = ⎛⎜ m ⎞⎟ D
⎝ 2zeV ⎠

11
How does the ion generation step
for TOF influence m/z analysis?

Consider MALDI

hυ
Matrix
Target

Analyte
Kinetic Energy distribution ?
Spatial distribution?

How will kinetic energy spread

influence appearance of spectrum?

Cotter

12
Solution to peak broadening caused by
kinetic energy spread:

Reflectron (ion mirror)

Series of ring electrodes, typically
with linear voltage gradient

13
 Time-of-Flight Reflectron
• Increased resolution via compensation for KE spread from the
source

http://www.jic.bbsrc.ac.uk/services/proteomics/tof.htm

Reflector TOF
Mass Analyzer Reflectron
(TOF)
Detector

Ion Source
(MALDI)

x x

x x
x

High Sensivity
High resolution
Large Mass Range
KE = ½ mv2

14
 http://www.abrf.org/ABRFNews/1997/June1997/jun97lennon.html

We talked about how

to deal with kinetic
energy spread.

How do we deal with

ions formed at
different locations in
the source (spatial
distribution)?

15
 Delayed Extraction
10 KV 10 KV

+ + + + +
+ + + + +

7 KV

High sensitivity
Low mass (below 40 k Da)
High resolution

Continuous vs. Delayed Extraction

Continuous TOF
Resolution = 700 (FWHM)

Delayed Extraction
Resolution = 6000 (FWHM)

16
 Recent TOF designs: improved resolution, better sensitivity and mass accuracy
(Ultraflex III MALDI TOF-TOF)
In te n s. [a .u .]

3145.708 * Pepmix\0_N6\1\1SRef
6000

5000 Resolution: 25,000

S/N: 46
4000

3000

2000
3177.722

1000

0
3140 3145 3150 3155 3160 3165 3170 3175 3180 3185
m/z

TOF Typical Specs

• m/z Range: unlimited u • Quantification: low -

• Resolution: ~20,000 medium
(Reflectron)
• Positive and
• Mass Accuracy: ~ 3-10
Negative Ions
ppm (300-4,000 u)
• Scan Speed: 106 u/s • Variations: Linear,
• Vacuum: 10-7 Torr Reflectron, Tandem
w/ quads, TOFs
and/or sectors

17
Can an MS/MS instrument be
constructed if the only analyzer
type available is TOF?

TOF-TOF

http://docs.appliedbiosystems.com/pebiodocs/00106293.pdf

18
 Activation:
High-energy (keV) Collisions
with Gas on a TOF-TOF

- Fragments of Glu-Fibrinogen
(m/z 1570.68 Da; 1 pmol)

Average resolution 4000

Mass accuracy < 0.05 Da

16O/18O-labeled DLEEGIQTLMGR

Medzihradszky, KF et al. Anal Chem. 2000, 72: 552-558

19
 x104

Intens. [a.u.]
328.574
6

492.623 981.346
5

4 186.600 656.765

146.669

3
821.038

120.694
1
284.552
90.771 941.468
443.572 612.695 721.026 776.938

0
200 400 600 800 1000
m/z

MALDI TOF-TOF fragmentation spectrum of a sodiated polymer

O CH2 CH2 *
m
O n
O

3-OEB, m=1-3 (164, 44)

Copolymer of 2-hydroxybenzoic acid and ethylene carbonate

TOF TOF
More
fragmentation
than QqQ
or trap

20
 Advantages and Disadvantages
Mass Spectrometer Advantages Disadvantages
TOF-TOF high resolution, high Large size
m/z fragment ions
Not ideal for
keV CID continuous
ionization source

easier de novo $$$

peptide sequencing
dn and wn to
distinguish Ile/Leu

Analyzers
Quadrupole
TOF

Quadrupole Ion trap

FTICR
Magnetic sector

21
 Quadrupole (Q)

Quadrupole (Q)
• four parallel rods or poles
• fixed DC and alternating RF voltages

rf voltage
+dc voltage
rf voltage 180° out of phase
-dc voltage
• only particular m/z will be focused on the
detector, all the other ions will be deflected into
the rods
• scan by varying the amplitude of the voltages
– (AC/DC constant).

22
 Quadrupole Field Animation
http://www.kettering.edu/~drussell/Demos/Me
mbraneCircle/Circle.html
Positive rod

Negative rod

Negative rod
Positive rod

negative DC offset

-DC

- positive DC offset
-

+DC

23
 Ion Motion in Quadrupoles
qualitative understanding

• + DC, ions focused to center

• - DC, ions defocused

• +DC w/ rf, light ions respond to rf,

eliminated (high mass filter)

• -DC w/ rf, light ions respond to rf,

focused to center (low mass filter)

TSQ 7000 TSQ Quantum

1993 to 2000 2001 to …

c/o ThermoFinnigan Corp.

24
RF only mode

25
Initial kinetic energy affects ion motion in quad

Quadrupole Typical Specs

• Quantification: good
• m/z Range: 2-4000 u choice
• Resolution: Unit • Positive and Negative
• Mass Accuracy: ca +/- Ions
0.1 u • Variations: SingleQ,
• Scan Speed: 4000 u/s TripleQ, Hybrids
• Vacuum: 10-4 – 10-5
Torr
• Low Voltages:
RF ~6000 –10000 V
DC ~500V-840V
Source near ground

26
 What MS/MS instruments can be
produced from Q?

What MS/MS instruments can be

produced from Q andTOF?

Triple Quadrupole
Since late 1970’s and still strong!

Attractive Features?
gSource near ground & operates at relatively
high pressure - couples well to sources, chromatography
gMultiple scan modes easy to implement

27
 Triple Quadrupole (QQQ)
Detection
System

Q3

Source QOO Q0 Q1

Q2
Dynode Turbo
Heated
Capillary
Q3

Q2

c/o Thermo Finnigan Corp. Q1 Q0 Q00

Quadrupole-Time-of-Flight (Q-TOF)

http://www.waters.com/WatersDivision/waters_website/products/micromass/ms_top.asp (outdated)

28
 Activation:
Low-energy (eV) Collisions
with Gas

Q-TOF

80 fmol BSA digest

QQQ

Shevchenko, A., et al., Rapid. Commum. Mass Spectrom., 1997, 11: 1015-1024

29
Analyzers: Traps
Quadrupole
TOF

Quadrupole Ion trap

FTICR
Magnetic sector

What is small, inexpensive

and still gives great MSMS ?????

Quadrupole Ion Traps

Miniature IT: Cooks, R. G. and coworkers
Anal. Chem. 2002, 74, 6145-6153; 2000, 72, 3291-3297.

30
 http://www.chem.wm.edu/dept/faculty/jcpout/faculty.html

Ion path in a trap

Quadrupole Ion Trap (QIT)

http://www-methods.ch.cam.ac.uk/meth/ms/theory/iontrap.html

31
 Quadrupole Ion Trap (QIT)
• Quadrupole ion trap mass analyzer consists of three
hyperbolic electrodes: the ring electrode, the
entrance endcap electrode and the exit endcap
electrode.
• Ions enter trap through inlet focusing system and
entrance endcap electrode.
• An AC potential of constant frequency and variable
amplitude is applied to the ring electrode to produce
a 3D quadrupolar potential field within the trapping
cavity which traps ions in a stable oscillating
trajectory confined within the trapping cell.
• The oscillating trajectory is dependent on the trapping
potential and the mass-to-charge ratio of the ions.
• During ion detection, the electrode system potentials
are altered to produce instabilities in the ion
trajectories and thus eject the ions.

Quadrupole Ion Trap (QIT)

32
 Activation:
Low-energy (eV) Collisions
with Gas

IRMPD
(Infrared Multiphoton Dissoc)

Research: Micro CIT Array

Matt Blain, Sandia
Cooks, Purdue
1.8 µm

2.4 µm

Top End Cap Array

Ring Electrode Array

Bottom End Cap Array
Collector Array

33
 QIT Typical Specs

• m/z Range: 20-6000 u • Quantification:

• Resolution: Unit possible, not accurate
• Mass Accuracy: ca +/- • Positive and
0.1 u
Negative Ions
• Scan Speed: 4000 u/s
• Vacuum: 10-3 Torr

Advantages and Disadvantages

Mass Spectrometer Advantages Disadvantages
QIT Compact Limited storage of
ions limits the
dynamic range of the
ion trap (space
charge effect)
MSn 1/3 of low mass
range lost in MS/MS
mode, typical
operation
Data dependent
scanning
Relatively Low E collisions
inexpensive

34
 Advantages and Disadvantages

Mass Spectrometer Advantages Disadvantages

QIT Poor quantification
Sensitive Collision energy not
well-defined in CID
MS/MS

Mass Accuracy

To increase mass accuracy in a

Trap Æ LT, orbitrap, FT-ICR

RF ION TRAP ELECTRODE

STRUCTURES

LCQ-Type 3D LTQ-Type (2D)

Quadrupole Trap Linear Quadrupole Trap

ASMS Fall Workshop

2006 JEPS

35
 Linear Ion Traps
Basic Linear Trap Structure

R0 = 4 mm
Hyperbolic Rods
X0 = 4.76 mm
Y0 = 4 mm
Back
Y Section
Center
Section
Z
Front Slot
Section
X

2D vs. 3D Ion Traps

Ion Transfer
Tube

Skimmer

Tube Lens

36
Estimating Relative Ion Storage Capacity
3D Ion vs Linear (2D) Quadrupole Ion Traps

3D RF Quadrupole 2D RF Quadrupole
Ion Trap Linear Ion Trap
z
z y

y L

x x

R3D R2D
~ Spherical Ion Cloud ~ Cylindrical Ion Cloud
ASMS Fall Workshop
2006 JEPS

Overall Performance Gains

LTQ 3D Traps Increase

•Trapping efficiency ~ 55-70% ~5% ~ 11-14x

•Detection efficiency ~ 50-100% ~50% ~ 1-2x
•Trapping capacity ~ 20,000 ions ~500 ions ~ 40x

37
 Motivating Factors Realized

• Increased Trapping Efficiency

• Increased Trapping Capacity

Which means....
• Increased Sensitivity
• Increased Inherent Dynamic Range
• Increased S/N for full Scan MS
• Practical MSn
•Faster Scan Times - no μscans (only one)

How are 3-D traps and linear

ion traps used in MS/MS
Stand alone
3-D traps
LTQ
Front or back end of tandem-in-space
LT-TOF
LT-FT, LT-Orbitrap,
QTrap

38
 LIT and QTrap;
QTrap; Different ways of using Linear Traps

Linear Ion Trap ~ 100% of ions trapped are

detected due to radial ejection

Skimmer

Axial ejection allows for hybridization

– without compromise (FT)!

Hybrid Quadrupole Trap Majority of trapped ions

cannot be scanned out
~ 15% detected*

Axial ejection depends on fringe fields generated by grid –

this grid compromises triple quadrupole performance

*Hager, J., RCM., 2003, 17, 1389

9 Protein Mixture
9 Protein Mixture Peptide Identification

80 73

70 61
Number of Peptides

60
50 42
35 Deca XP plus
40 31
24
LTQ
30 21

20 12

10
0
10min 20min 30min 60min
Gradient (min)

39
 Activation:

CID
Low-energy (eV) Collisions
with Gas

IRMPD
(Infrared Multiphoton Dissoc)

ETD
(electron transfer dissociation)

Analyzers
Quadrupole
TOF

Quadrupole Ion trap

FTICR
Magnetic sector

40
 Analyzers based on magnetic fields: sector, ICR

Magnetic forces move ions in a circular path

demo http://www.casetechnology.com/implanter/magnet.html

For a charge q moving in a magnetic field B

there exists a force z to v and B

figures http://physics.unr.edu/faculty/phaneuf/classinfo/p181wk11.pdf

41
 Read on your own

Scan B

Analyzers
Quadrupole
TOF

Quadrupole Ion trap

FTICR

Magnetic sector

Orbitrap

42
 v

Fcp

Fcp = q [vxB]
B

Cyclotron motion of an ion in a magnetic field (B). The magnetic

field points out of the plane.
Note: ion motion is much more complex due to the presence of
electrostatic field (magnetron/cyclotron motion)

RF-excitation

Ion Detection Plates

Ion Detection Plates

Note: for clarity, the front and back trapping plates are not shown

43
 Fourier Transform-Ion Cyclotron
Resonance (FTICR)
• In the presence of a magnetic field, sample
ions orbit according to cyclotron frequency, fc
• Cyclotron frequency related to charge of ion
(z), magnetic field strength (B) and mass of
ion (m).

• All ions of same m/z will have same cyclotron

frequency at a fixed B and will move in a
coherent ion packet.

FTICR
• Image is Fourier transformed to obtain the component
frequencies and amplitudes (intensity) of the various ions.
• Cyclotron frequency value is converted into a m/z value to
produce mass spectrum w/ the appropriate intensities.

44
a

time (ms)
C9H16N5
b 194.1405
c

C11H20N3
194.1657
C7H12N7
194.1154

45
 Fourier Transform-Ion Cyclotron
Resonance (FTICR)
• Ion packets produce a detectable image current on the
detector cell plates.

• As the ion(s) in a circular orbit approach the top plate,

electrons are attracted to this plate from ground. Then as the
ion(s) circulate towards the bottom plate, the electrons travel
back down to the bottom plate. This motion of electrons
moving back and forth between the two plates produces a
detectable current.

46
 FTICR Typical Specs

• m/z Range: > 15000 u • Quantification:

• Resolution: High, 106 possible, not accurate
• Mass Accuracy: 100 • Positive and
ppb
Negative Ions
• Scan Speed: fast
• Vacuum: 10-7- 10-9 Torr

11+

12+

10+

9+

47
Charge state/MW determination
for proteins

Δm = z
Δ(m/z)

Carbons
isotopes so
Δm=1 Da

Calc Δ(m/z)

Finnigan LTQ FT
Linear Ion Trap MS FTICR MS
• MS, MS/MS and MSn Analysis • Ion Image Current Detector
• AGC Control • Accurate Mass, High Resolution
• Secondary Electron Multiplier Detector • ECD, IRMPD
FTMS Data

Linear Ion Trap Data 7 T Actively Shielded

Superconducting Magnet

ECD Assembly
60m3/hr 15L/s 300L/s 400L/s 210L/s 210L/s
IRMPD Laser Assembly

Triple Ported Turbo Pump

48
 Workflow

Introducing the New apex®-ultra

Hybrid Qq-FTMS
Announced at PittCon 2007 in Chicago, IL

• The new apex-ultra

combines ease-of-use
with power and versatility

• Improved electronics for

substantial gains in
analytical performance
and capabilities

• Comprehensive software
tools that are specifically
designed for protein
characterization

49
 Versatility matched with Performance
The apex®-ultra
h1 Q1 h2

to analyzer

ESI source region ECD / IRMPD

Masses
Masses can
can be
be filtered
filtered
here
here in
in a
a results-driven,
results-driven,
targeted approach
targeted approach
Ions
Ions accumulated
accumulated herehere
CASI provides the means to enrich or amplify to
to build
build significant
significant
low abundant species for subsequent populations an in-cell
populations an in-cell
fragmentation and analysis event
event (e.g.
(e.g. ECD)
ECD)

Continuous Accumulation of Selected Ions – “CASI”

Activation:
SORI CID
Low-energy (eV) Collisions
with Gas (off resonance)
RE
(resonance excitation)
IRMPD
(Infrared Multiphoton Dissoc)
ECD
(electron transfer dissociation)

50
 Intens. YIGSR_QCID_22eV_000002.d: +MS2(595.0)
x107
3.0
MH+ 249.1593
595.3171
2.5
QCID 22 eV
MS/MS spectra depend
2.0

on
i) Charge state
1.5 302.1453

ii) Ion activation method 1.0

175.1186
560.2803
iii) Collision energy 0.5
408.1864
465.2077
90.2256
0.0
x108 YIGSR_doubly_QCID_6eV_000001.d: +MS2(298.0)

(more details in the [M+2H]2+ 319.1718

1.5
Ion Activation QCID 6 eV
Methods
1.0
by Vicki Wysocki)
249.1593

0.5
y5
277.1541 432.2552
136.0756
0.0
x107 YIGSR_doubly_IRMPD_40P_0_30s_000001.d: +MS2(298.0)

2.0 [M+2H]2+ 298.2804

IRMPD 30s, 30%

1.5

1.0

249.1644

0.5

102.7325 595.3466
0.0
100 200 300 400 500 600 m/z

Advantages and Disadvantages

Mass Spectrometer Advantages Disadvantages
FTICR Highest recorded Limited Dynamic
mass resolution of all Range
mass spectrometers
MSn Low E collisions
Non-destructive ion High vacuum
detection Low presure
(difficult GC/LC
coupling)
Accurate mass Big size
measurement
Powerful capabilities Not a high
for ion chemistry throughput technique
experiments (ion-
molecule rxns)

51
Orbitrap

Orbitrap

52
 LTQ Orbitrap™ Hybrid MS
Finnigan LTQ™ Linear Ion Trap

API Ion source Linear Ion Trap C-Trap

Orbitrap
Differential pumping

Differential pumping

LTQ Orbitrap Hybrid MS

System Integration
Finnigan LTQ™ Linear Ion Trap

Gas <1 mtorr

-2 k V

Central
Electrode
Voltage

-3.5 k V

53
 Lord of the ion rings: Retainment of the rings
Image current detection on
split outer electrodes

k
ω=
m/ z

1. Frequencies are determined using a Fourier Transformation

2. For higher sensitivity AND resolution, transients should not decay too fast

Ultra-high vacuum Ultra-high precision

Thermo slide

Ion Motion in the Orbitrap

Simulation
Simulationof
ofion
iontrajectory
trajectorywith
withSIMION
SIMION

Characteristic
Characteristicfrequencies
frequencies 2
ωz ⎛ Rm ⎞
ωϕ = ⎜ ⎟ −1
– Frequency of rotation ωφ 2 ⎝ R ⎠
2
⎛ Rm ⎞
– Frequency of radial oscillations ωr ωr = ω z ⎜ ⎟ −2
⎝ R ⎠

k
– Frequency of axial oscillations ωz ωz =
m/q

54
 Orbitrap --Resolving Power
Insulin:m/z
Insulin: m/z==5733
5733
+5 Charge
Chargestate:
state:+5,
+5,+4
+4and
and+3
+3

+3
+5
m/Δm = 70,000 +4

1,200 1,400 1,600 1,800 2,000

m/z
+4
1,147 1,148 1,149
m/z
m/Δm = 45,000
+3

m/Δm = 40,000

1,434 1,435 1,436

m/z

R. Noll, H. Li, 2002 1,911 1,912 1,913 1,914

m/z

Question: Consider an ion source block and an

extraction lens. How would you bias the block and
lens if you want the ions to be accelerated by

a) 8000 eV (appropriate for magnetic sector)

b) 5 eV (appropriate for entering a quadrupole)

c) 20,000 eV (appropriate for entering a TOF)

55
 Learning Check
Draw the appearance of the mass spectrum in which
both singly and doubly charged YGGFLR (molecular
weight 711.3782) are produced and analyzed with a
quadrupole, TOF and FT-ICR (Hint: peaks widths
important)

TOF
Single & Doubly
charged YGGFLR
Intensity

Quad m/z

FT-ICR
Intensity

Intensity

m/z

m/z

56
 • No instrument ideal (many are
complementary)
• Assess your needs
» Assess your budget

• Build your own

Suggested Reading List

GENERAL MS AND MS/MS

Kinter, M. and Sherman, N. E., Protein Sequencing and Identification Using Tandem
Mass Spectrometry,
Wiley and Sons, New York, NY, 2000.
De Hoffmann E., Mass Spectrometry – Principles and Applications (Second
Edition), Wiley and Sons,
New York, NY, 2002.
Busch, K.L., et al., Mass spectrometry/ mass spectrometry: techniques and
applications of tandem
mass spectrometry, VCH Publishing, New York, NY, 1988.
McLafferty, F.W. (Ed) Tandem Mass Spectrometry, Wiley and Sons, New York, NY,
1983.
McLafferty, F.W. and Turecek, F. Interpretation of Mass Spectra, University Science
Books, New York, NY, 1993.
Siuzdak, G. Mass Spectrometry for Biotechnology, Academic Press, San Diego, CA,
1996.
Gygi, S.P. and Aebersold, R., Curr. Opin. Chem. Biol., 4 (5): 489, 2000.
Roepstorff, P., Curr. Opin. Biotech., 8: 6, 1997.
De Hoffmann, JMS, 31: 129, 1996.
Mann, M. et al., Annu. Rev. Biochem., 70: 437, 2001.
McLuckey, S and Wells, J.M., Chem. Rev., 101: 571, 2001.

57
 Suggested Reading List
Q-TOF

Morris, H.R. et al., J. Protein Chem., 16: 469, 1997.

Shevchencko A., et al., Rapid Commun. Mass Spectrom., 11: 1015, 1997.
Shevchencko A., et al., Anal. Chem., 72: 2132, 2000.
Medzihradszky, K.F., et al., Anal. Chem., 72: 552, 2000.
Glish, G.L. and Goeringer, D.E., Anal. Chem., 56: 2291, 1984
Morris, H.R. et al., Rapid Commun. Mass Spectrom., 10: 889, 1996.
Wattenberg, A. et al., JASMS, 13 (7): 772, 2002.
Lododa, A.V. et al., Rapid Commun. Mass Spectrom., 14(12): 1047, 2000.

TOF

Bush, K., Spectroscopy, 12: 22, 1997.

Cotter, R.J., Time-of-Flight: Instrumentation and Applications in Biological
Research, ACS, Washington, DC, 1994.

Suggested Reading List

TOF-TOF

Yergey, A.L. et al., JASMS, 13 (7): 784, 2002.

Go, E.P. et al., Anal. Chem., 75: 2504, 2003.

FTICR

Buchanan, M.V. (Ed), Fourier Transform MS, ACS, Washington, DC, 1987.
Comisarow, M.B. and Marshall, A. G., Chem. Phys. Lett., 25: 282, 1974.
McIver, R.T. et al., Int. J. Mass Spectrom. Ion Processes, 64: 67, 1985.
Kofel, P. et al., Int. J. Mass Spectrom. Ion Processes, 65: 97, 1985.
Williams, E. R. Anal. Chem., 70: 179A, 1998.
McLafferty, F. W. Acc. Chem. Res., 27: 379, 1994.
Fridriksson, E. K. et al., Biochemistry, 39: 3369, 2000.
Fridriksson, E. K. et al., Biochemistry, 38: 8056, 1999.
Kelleher, N. L.et al., Protein Science, 7: 1796, 1998.
McLafferty, F. W. et al., Int. J. Mass Spectrom., 165: 457, 1997.
.

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 Suggested Reading List
Green, M. K. and Lebrilla, C. B. Mass Spectrom. Rev., 16: 53, 1997.
Guan, S. and Marshall, A. G. Chem. Rev., 94: 2161, 1994.

QIT

Marsh, R.E. et al., Quadrupole Storage Mass Spectrometry, vol.102, Wiley

and Sons, New York, NY, 1989.
Cooks, R.G. et al., Ion trap mass spectrometry. Chem. Eng. News, 69(12):
26, 1991.
Jonscher, K.R. et al., Anal Biochem, 244(1): 1, 1997.
Louris, J.N. et al., Anal. Chem., 59(13): 1677, 1987.
Louris, J.N. et al., Int. J. Mass Spectrom. Ion Processes, 96(2): 117 1990.
Cooks, R.G. et al., Int. J. Mass Spectrom. Ion Processes, 118-119: 1 1992.
McLuckey, S. A. et al., Int. J. Mass Spectrom. Ion Processes, 106: 213, 1991.
Ngoka, L. C. M. and Gross, M. L. Int. J. Mass Spectrom. 194: 247, 2000.

Suggested Reading List

QQQ

Yost, R. A. and Enke, C. G. J. Am. Chem. Soc., 100: 2274, 1978.

Arnott, D. in Proteome Research: Mass Spectrometry, james, P (Ed.), pp 11-
31, Springer-Verlag, Germany, 2001.
Steen H. et al., JMS, 36: 782, 2001.
Miller, P.E. and Denton, M.B., J. Chem. Educ., 7: 617, 1986.
Yang, l. et al., Rapid Commun. Mass Spectrom., 16(21): 2060, 2002.
Mohammed, S. et al., JMS, 36: 1260, 2001.
Dongre, A.R. et al., JMS, 31: 339, 1996.

Orbitrap

Hu, Q, Noll, RJ, Li, H., Makarov, A., Hardman, M., Cooks, R.G. JMS, 430-
443, 2005.

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