MS Course Mass Analyzers Class1

8/6/2019 MS Course Mass Analyzers Class1

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Mass Analyzersrpd Somogyi

Chemistry and Biochemistry MassSpectrometry Facility

Universit Joseph Fourier, Grenoble, November 19, 2010

Want to do MS or MS/MS ?Need a Mass Spectrometer

Ionizationsource

Massanalyzer

Detector

inlet all ions sortedions

Datasystem


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Ionizationsource

Massanalyzer

Detector

ions

a asystem

Ion movement Charged metal plates (electrodes, lenses) used

Electrodes and physical slits used to shape andrestrict ion beam

Good sensitivit is de endent on ood iontransmittance efficiency in this area

inlet all ions

Ionizationsource

Massanalyzer

sortedions

Detector

Datasystem


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Ion detection

Ions can be detected efficiently w/ high

that eject electrons

inlet all ions

Ionizationsource

Massanalyzer

sortedions

Detector

Datasystem

Kinetic energy of ions defined by

Ion energy

E = zeV = qV = mv2

E = kinetic energy

m = mass

v = velocitye = electronic charge (1.60217e-19 C)

z = nominal charge

V = accelerating voltage


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Learning Check

Consider two electrodes,

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

1000V 0 V

+ ion will travel with kinetic energy of___________

Mass spectrometers separate ions with a

Mass Resolution

defined resolution/resolving power

Resolving power- the ability of a massspectrometer to separate ions with

eren mass o c arge m z ra os.


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M

Resolution defined at 10% valley

R=M/M

M

Example of ultrahigh resolutionin an FTICR

J. Throck Watson Introduction to Mass Spectrometry p. 103


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General about mass

spectrometers

Common features

Accelerated charge species (ions) interactwith

Electrostatic field (ESA, OT)

Ma netic field B ICR

Electromagnetic (rf) fields (Q, IT, LT)

Or ions just fly (TOF)

1) They should sort ions by m/z

Desirable mass spectrometercharacteristics

2) They should have good transmission (improvessensitivity)

3) They should have appropriate resolution (helpsselectivity)

4) They should have appropriate upper m/z limit

5) They should be compatible with source output(pulsed or continuous)


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For each of the following applications, choose the mostappropriate mass analyzer from the following list. Use eachanalyzer only once.

orbitrap (OT) 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)_______

confirmation of benzene in extracts from 3000

soil samples_______ Petroleum chemist wants to confirm the

presence of 55 unique compounds at onenominal mass/charge value in a mass spectrum

m/z values are determined by actually measuring different

Mass spectrometers record m/zvalues

Type of analyzer electric sector

magnetic sector

Physical parameter used asbasis for separation kinetic energy/z

momentum/z

p ys ca parame ers

quadrupole, ion trap time-of-flight

FT-ion cyclotron resonance

m/z flight time

m/z (resonance frequencies)


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Magnetic (B) and/or Electrostatic (E) (HISTORIC/OLDEST)

Time-of-flight (TOF)

Types of Mass Analyzers

Quadrupole (Q)

Quadrupole Ion Trap (IT)

Linear Ion Trap (LT)

Orbitrap

Fourier Transform-Ion Cyclotron Resonance (ICR)

Performance Advantages / Disadvantages / $$$

TOF

Quadrupole

Quadrupole Ion trap

FTICR

Orbitrap


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

High voltage (keV energy range)

magne

electrostatic (E)

time-of-flight (TOF)

quadrupole (Q)

ion trap (IT, LT)

ion cyclotron resonance (ICR)

IonizationIonization AnalysisAnalysis

MS and MS/MS revisited

MS:

Collide withtarget to producefragments

Collide with

fragments

MS/MS:

Ionization

MS/MS:

Ionization AnalysisAnalysisSelectionSelection ActivationActivation


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

Tandem in Space

Current popular MS/MSarrangements (2009)

q

Q Trap

Q TOF

TOF TOF

Tandem in Time

Ion Trap (2 or 3 D)

FT-ICR (FT)


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Decision factors when choosing a

mass spectrometer

S p e e e e e e e e e e e e e d

R e s o l u t i o n Sensitivity

r Co$t


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TOFQuadrupole

Quadrupole Ion trap

FTICR

Orbitrap

D

tor

Time of Flight

KE = zeV = mv2 m = massV = velocity

v = D/t D = distance of flight

m/z

V

Dete

t = time of flightm(D/t)2 = zeV KE = kinetic energy

e = charge

D=t

21

2zeVm

/


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How does the ion generationstep in TOF influence m/z

analysis?

Matrix

h

et

Analyte+

Targ

Analyte ion may have (1) Kinetic Energydistribution or (2) Spatial distribution

How will KE spread influencethe spectrum?

Ions of same

Hasslightlygreater KE

Effect is broadpeaks

c/o Cotter


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Solution to peak broadening caused by

How will KE spread influencethe spectrum?

kinetic energy spread:

Reflectron (ion mirror)

Series of ring electrodes, typicallywith linear voltage gradient

Increased resolution by compensating for KE spread from thesource

Time-of-Flight Reflectron

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


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Ion Source

Detector

Mass Analyzer

(TOF)

Reflectron

Reflectron TOF

xx

x

x x

(MALDI)

KE = mv2

High resolution

Ion Source

Detector

Mass Analyzer(TOF)

ReflectronReflectron TOF

x

(MALDI)

KE = mv2

High resolution


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

We talked about howto deal with kineticenergy spread.

How do we deal withions formed atdifferent locations inthe source (spatialdistribution)?


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10 KV 10 KV

Delayed Extraction

+

+

+

+

7 KV

++

++

+

+

Low mass (below 40 k Da)High resolution

Continuous TOF

Resolution = 700 (FWHM)

Continuous vs. Delayed Extraction

Delayed Extraction

Resolution = 6000 (FWHM)


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3145.708 * Pepmix\0_N6\1\1SRef

5000

6000

In

te

n

s.

[a

.u.

]

Recent TOF designs: improved resolution, better sensitivity and mass accuracy(Ultraflex III MALDI TOF-TOF)

Resolution: 25 000

3177.722

1000

2000

3000

4000

S/N: 46

03140 3145 3150 3155 3160 3165 3170 3175 3180 3185

m/z

m/zRange: unlimited u

~

Quantification: low -

Typical TOF Specs

,(Reflectron)

Mass Accuracy: ~ 3-10ppm (300-4,000 u)

Scan Speed: 106 u/s

Vacuum: 10-7 Torr

Positive andNegative Ions

Variations: Linear,Reflectron, Tandem

,and/or sectors


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constructed if the only analyzer

type available is TOF?

TOF-TOF

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


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TOF TOF(high energy, keV, collisions)

More

ragmen a on

than QqQ

or trap

(low energy,e , co s ons

Mass Spectrometer Advantages Disadvantages

TOF-TOF high resolution, high Large size

Advantages and Disadvantages

m/z fragment ions

keV CID

Not ideal forcontinuous

ionization source

easier de novopeptide sequencing

$$$

dn and wn todistinguish Ile/Leu


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TOFQuadrupole

Analyzers

Quadrupole Ion trap

FTICR

Orbitrap


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Quadrupole (Q)

four parallel rods or poles

fixed DC and alternating RF voltages

Quadrupole (Q)

rf voltage+dc voltage

rf voltage 180 out of phase-dc voltage

on y part cu ar m z w e ocuse on t edetector, all the other ions will be deflected intothe rods

scan by varying the amplitude of the voltages

(AC/DC constant).


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Positive rod

Quadrupole Field Animation

Negative rod

http://www.kettering.edu/~drussell/Demos/MembraneCircle/Circle.html

Positive rod Negative rod

negative DC offset

+

+

-- positive DC offset

-DC

+DC


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+ DC, ions focused to center

Ion Motion in Quadrupoles- a qualitative understanding

- DC, ions defocused

+DC w/ rf, light ions respond to rf, eliminated(high mass filter)

-DC w/ rf, light ions respond to rf, focused tocenter(low mass filter)

TSQ 70001993 to 2000

TSQ Quantum2001 to

c/o ThermoFinnigan Corp.


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Quadrupole animation

http://www.youtube.com/watch?v=8AQaFdI1Yow&feature=related

QuickTime and aTIFF (LZW) decompressor

are needed to see this picture.


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RF only mode

Initial kinetic energy affects ion motion in quad


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m/zRan e: 2-4000 u Quantification: good

Quadrupole Typical Specs

Resolution: Unit Mass Accuracy: ca +/-

0.1 u

Scan Speed: 4000 u/s Vacuum: 10-4 10-5

Torr

Positive and NegativeIons

Variations: SingleQ,TripleQ, Hybrids

Low Voltages:

RF ~6000 10000 VDC ~500V-840V

Source near ground

What MS/MS instruments can be

What MS/MS instruments can beproduced from Q and TOF?


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Triple Quadrupole- since 1970s and still going strong!

Q1 Q2 Q3

S D

Attractive Features:

Source near ground and operates at relatively high pressure

Couples well to source and to chromatographyMultiple scan modes easy to implement

DetectionSystem

Q3

Dynode Turbo

Triple Quadrupole (QQQ)

Source

HeatedCapillary

Q2

Q1Q0

c/o Thermo Finnigan Corp.

Q3

Q2

Q1 Q0 Q00

c/o Agilent Corp.


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Quadrupole Time of Flight(Q-TOF)

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

Low-energy (eV) Collisionswith Gas

The third Q in QQQ is replacedby a TOF

Advantages?


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Q-TOF

80 fmol BSA digest

QQQ

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

Ion Mobility in a Q-TOF - Animation

http://mass-spec-blog.blogspot.com/2007/09/ion-mobility-separation-animation.html


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Another important use of a modified Q-TOF:

Ion Mobility

http://mass-spec-blog.blogspot.com/2007/09/ion-mobility-separation-animation.html

Selection of [M+2H]+2 at m / z246.1

600

500

400

100

80enisty

300

200

100

m/z

SDGRGGRGDS

40

20

0RelativeIn

76543210Drift Time (ms)


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Transfer CID of [M+2H]+2 at m / z246.1

3.0

ime(ms)

100eAbundance

100

50

0

.

2.0Drift

dt = 2.68-2.83 ms

SDGRG

b4

RSi

y4y3

50

0

Relativ

500400300200100

m / z

dt = 2.49-2.68 ms

GRGDS

b3

b2

y1

R

Si

UL_110510_GNR.raw : 1


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140

150

)

Corrected Cross Sections (A2) as a Function of m/z for SinglProtonated GnR (n=1-7)

G7R

100

110

120

130

libratedCrossSections(A

G4R

200 250 300 350 400 450 500 550 600

90

C

m/z

GR


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TOFQuadrupole

Analyzers

Quadrupole Ion trap

FTICR

Orbitrap

What is small, inexpensiveand still gives great MSMS ?????

Quadrupole Ion TrapsMiniature IT: Cooks, R. G. and coworkers

Anal. Chem. 2002, 74, 6145-6153; 2000, 72, 3291-3297.


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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


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Quadrupole ion trap mass analyzer consists of threehyperbolic electrodes: the ring electrode, theentrance end cap electrode and the exit endcape ec ro e.

Ions enter trap through inlet focusing system andentrance endcap electrode.

An AC potential of constant frequency and variableamplitude is applied to the ring electrode to producea 3D quadrupolar potential field within the trappingcavity which traps ions in a stable oscillating

. The oscillating trajectory is dependent on the trapping

potential and the mass-to-charge ratio of the ions. During ion detection, the electrode system potentialsare altered to produce instabilities in the iontrajectories and thus eject the ions.



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3D - Quadrupole Ion Trap (Demo)

Activation:Low-energy (eV) Collisions

w as

IRMPD(Infrared Multiphoton Dissoc)


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Research: Micro CIT ArrayResearch: Micro CIT Array

Matt Blain, SandiaCooks, Purdue

. m

2.4 m

Top End Cap Array

Ring Electrode Array

Bottom End Cap Array

Collector Array

QIT Typical Specs

m/zRange: 20-6000 u Quantification:

Mass Accuracy: ca +/-0.1 u

Scan Speed: 4000 u/s

Vacuum: 10-3 Torr

,



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QIT Compact Limited storage of ions limits the


ion trap (spacecharge effect)

MSn 1/3 of low massrange lost in MS/MS

mode, typicaloperation

scanning

Relativelyinexpensive

Low E collisions


QIT Poor uantification


Sensitive Collision energy notwell-defined in CIDMS/MS

Mass Accuracy

To increase mass accuracy in aTrap LT, orbitrap, FT-ICR


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RF ION TRAP ELECTRODESTRUCTURES

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

ASMS Fall Workshop2006 JEPS


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2D vs. 3D Ion Traps

Skimmer

Ion Transfer

Tube

Tube Lens

Linear Trap Demo

Skimmer

Ion Transfer

Tube

Tube Lens


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Overall Performance GainsOverall Performance Gains

Trapping efficiency

Detection efficiency

Trapping capacity

~ 50-100% ~50% ~ 1-2x

~ 55-70% ~5% ~ 11-14x

~ 20,000 ions ~500 ions ~ 40x

Increased Trapping Efficiency

Increased Trapping Capacity

Motivating Factors Realized

Increased Sensitivity

Increased Inherent Dynamic Range

Which means....

ncrease or u can Practical MSn

Faster Scan Times - no scans (only one)


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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

Skimmer

~ 100% of ions trapped aredetected due to radial ejection

Linear Ion Trap

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

Axial ejection allows forhybridization without compromise (FT)!

Hybrid Quadrupole Trap

~ 15% detected*

Majority of trapped ionscannot be scanned out

Axial ejection depends on fringe fields generated by grid this grid compromises triple quadrupole performance

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


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Activation:

CID-

with Gas

IRMPD

ETD(electron transfer dissociation)


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TOFQuadrupole

Analyzers

Quadrupole Ion trap

FTICR

Orbitrap

Cyclotron motion of an ion in a magnetic field (B).Note: ion motion is much more complex due to the presence ofelectrostatic field (magnetron/cyclotron motion, see below)


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Ion Detection Plates

RF-excitation

B

v

Ion Detection Plates

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


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In the presence of a magnetic field, sampleions orbit accordin to c clotron fre uenc f

Fourier Transform-Ion Cyclotron

Resonance (FTICR)

Cyclotron frequency related to charge of ion(z), magnetic field strength (B) and mass ofion (m).

All ions of same m/z will have same cyclotronfrequency at a fixed B and will move in acoherent ion packet.


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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.

a

b c194.1405

C9H16N5time (ms)

194.1657

194.1154

C11H20N3

C7H12N7


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If the frequency is slightly off,The excitation is called SORI (sustained off-resonance irradiation)

FTICR animation

http://www.youtube.com/watch?v=a5aLlm9q-Xc&NR=1

QuickTime and aTIFF (LZW) decompressor

are needed to see this picture.


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FTICR Typical Specs

m/zRange: > 15000 u6

Quantification:,

Mass Accuracy: 100ppb

Scan Speed: fast

Vacuum: 10-7- 10-9 Torr

,


11+

10+

12+

9+


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Charge state/MW determination

for proteins

m = z(m/z)

Carbonsisotopes som=1 Da

Calc(m/z)

FTMS Data

Finnigan LTQ FTLinear Ion Trap MS MS, MS/MS and MSn Analysis AGC Control Secondary Electron Multiplier Detector

FTICR MS Ion Image Current Detector Accurate Mass, High Resolution ECD, IRMPD

7 T Actively Shielded

Superconducting Magnet

Linear Ion Trap Data

210L/s60m3/hr 300L/s 400L/s 210L/s15L/s

Triple Ported Turbo Pump

ECD Assembly

IRMPD Laser Assembly


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The new apex-ultra- -

Introducing the New apex-ultraHybrid Qq-FTMS

Announced at PittCon 2007 in Chicago, IL

with power and versatility

Improved electronics forsubstantial gains inanalytical performanceand capabilities

Comprehensive softwaretools that are specificallydesigned for proteincharacterization

Versatility matched with Performance

The apex-ultra

Q1 h2h1

Masses can be filteredhere in a results-driven,targeted approach

ESI source region ECD / IRMPD

Ions accumulated hereto build significantpopulations an in-cellevent (e.g. ECD)

Continuous Accumulation of Selected Ions CASI

CA SI p rov ides the means to en r i ch o r am p l i f y l ow abundan t spec ies fo r subsequen t f ragm en ta t ion and ana lys is


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Bruker 9.4 T FT-ICR Apex-Qh Tandem Mass Spectrometer

MALDIDual source, MS only, no ion selection

ESI

QCID (eV) MS/MS

Ion selection and activation in the ICR

IRMPD, SORI, ECD

HDX in the ICR cell


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Activation:

SORI CIDLow-energy (eV) Collisionswith Gas (off resonance)

RE(resonance excitation)

IRMPD(Infrared Multiphoton Dissoc)

ECD(electron transfer dissociation)

90.2256

175.1186

249.1593

302.1453

408.1864465.2077

560.2803

595.3171

YIGSR_QCID_22eV_000002.d: +MS2(595.0)

0.0

0.5

1.0

1.5

2.0

2.5

3.0

7x10

Intens.

1 : +81

MH+

QCID 22 eVMS/MS spectra depend

oni) Charge stateii) Ion activation methodiii) Collision energy

136.0756

249.1593

277.1541

319.1718

432.2552

_dou y_ _ e _ 1.d: + ( .

0.0

0.5

1.0

1.5

x1

YIGSR_doubly_IRMPD_40P_0_30s_000001.d: +MS2(298.0)7x10

[M+2H]2+

QCID 6 eV

y5

(more details in theIon ActivationMethodsby Vicki Wysocki)

100 200 300 400 500 600 m/z100 200 300 400 500 600 m/z

102.7325

249.1644

.

595.34660.0

0.5

1.0

1.5

2.0

100 200 300 400 500 600 m/z

IRMPD 0.3s, 30%


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Mass Spectrometer Advantages DisadvantagesFTICR Highest recorded

mass resolution of allLimited Dynamic

Range


mass spectrometers

MSn Low E collisions

Non-destructive iondetection

High vacuum

Low presure

(difficult GC/LCcoupling)

Accurate massmeasurement

Big size

Powerful capabilitiesfor ion chemistryexperiments (ion-

molecule rxns)

Not a highthroughput technique


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TOFQuadrupole

Quadrupole Ion trap

Magnetic sector

FTICR

Orbitrap

Orbitrap


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Orbitrap

LTQ Orbitrap Hybrid MSFinnigan LTQ Linear Ion Trap

API Ion source Linear Ion Trap C-Trap

Differential pumping

Differential pumping


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LTQ Orbitrap Hybrid MSSystem Integration

Gas


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Ion Motion in the Orbitrap

Simulation of ion trajectory with SIMIONSimulation of ion trajectory with SIMION

2

Rm2

RmCharacteristic frequenciesCharacteristic frequencies

Frequency of rotation

Frequency of radial oscillations r

Frequency of axial oscillations z

2

=R

2

=R

2

2

=R

Rmzr

2

2

=R

Rmzr

qm

kz

/=

qm

kz

/=

Insulin: m/z = 5733

Charge state: +5, +4 and +3

Insulin: m/z = 5733

Charge state: +5, +4 and +3

Orbitrap --Resolving Power

+

+5

+3

m/z1,1491,1481,147

+4

m/z2,0001,8001,6001,4001,200

+4m/m = 70,000

m/m = 45,000

m/z1,4361,4351,434

m/z1,9141,9131,9121,911

+3

m/m = 40,000

R. Noll, H. Li, 2002


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Question: Consider an ion source block and anextraction lens. How would you bias the block andlens if you want the ions to be accelerated by

b) 5 eV (appropriate for entering a quadrupole)

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


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Learning Check

Draw the appearance of the mass spectrum in whichboth singly and doubly charged YGGFLR (molecular.

quadrupole, TOF and FT-ICR (Hint: peaks widthsimportant)

712 in Quad, TOF, ICR

sity

TOF

m/z

Intensity

Inten

QUAD

ICR

m/z

m/z

Intensity


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Instrument Performance for Proteomic Applications

Han et al., Curr. Opin. Chem. Biol. 2008; 12(5):483-490.


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Many instruments are complementary

,

Assess your needs

Assess your budget

@ Research level, may want to buildyour own

Suggested Reading ListGENERAL 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 tandemmass 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.


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Suggested Reading ListQ-TOF

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

ShevchenckoA. et al. Ra idCommun. MassS ectrom., 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 ListTOF-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 ListGreen, 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 ListQQQ

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, 2001Miller, 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.Makarov A. Anal. Chem. 2000; 72(6):1156-1162.

Makarov A, Denisov E, Kholomeev A, Baischun W, Lange O, Strupat K, Anal. Chem. 2006; 78(7):2113-2120.

Makarov A, Denisov E, Lange O, Horning S. JASMS. 2006; 17(7):977-982.

Macek B, Waanders LF, Olsen JV, Mann M. Mol. Cell. Proteom. 2006; 5(5):949-958.

Perry RH, Cooks RG, Noll RJ. Mass Spectrom. Rev. 2008; 27(6):661-699.

Documents

MS Course Mass Analyzers Class1