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Mass Spectrometry and Protein Structure

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Mass Spectrometry and Protein Structure In dian Journal of Bi ochemistry & Bi ophys ics Vo L 39. August 2002. pp. 205-2 16 Minireview Mass spectrometry and protein structure Kapil Maith al' and K Muralidhar2* 'Dr. B R Ambedkar Center for Biomedi cal Research. 2Department of Zoology. Uni ve rsity of Delh i. Delhi 11 0007, India Received 24 April 2002; accepled 6 lillie 2002 Historical Overview ha s led to the usage of cesium (Cs) instead of atom Today's mass spectrometer is based on the seminal gun . wo rk performed by Sir J. J. Thomson of the Another method that all owed analys is of large, Cavendi sh Laboratory (Uni versity of Cambridge), non-volatil e orga nic molecul es was plasma­ whi ch led to the di scovery of the electron in 1897 and desorpti on mass spectrometry (POMS) developed by 5 6 also led to the first mass spectrometer whil e he was Torgerson et al. in 1974 . Wi th the advent of th is measuring the effects of electric and mag neti c fie ld s tec hnique analysis of proteins also became poss ible 7 on ions ge nerated by residual gases in cathode ray and in 1982 first ma ss spectrum of in sulin wa s tubes. Thomson noti ced that the ions move th rough recorded. This was soon foll owed by FAB mass 8 9 pa raboli c trajectori es proporti onal to their "mass-to­ spectra of in sulin . In spite of these ac hievements. charge" rati os. Thomson received the 1906 Nobel both the techniques had maj or limitations, li ke it wa s Pri ze in Phys ics "in recogniti on of the great merits of difficult to ex tend the detecti on mass range beyond 25 his theoreti ca l and experimental in vesti gati ons on the kOa and it was useful for a few ideall y behaved conduct ion of electric ity by gases". The time period proteins onl y. Further, sensiti vity of pi comole ran ge from the late 1930's can be consi dered the era, which was not as good as desired and analys is of mi xtures saw major breakthroughs in the field of mass was difficu lt due to suppression effec ts. spectrometry. But it was onl y around 1950 that mass This led to constant development and in mid j 980's spectromet ric (MS) analysis of peptides came into two new techniques were developed viz. electrospra y exi stence. The onl y shortcoming at that time wa s that ion ization (ESJ) and matri x assisted laser the onl y ionization method ava il able was electron desorpti on/ioni za ti on (MALDI), whi ch had a impact and it requi red extensive derivatizati on of the sign ifica nt impact on the capabilities of mass peptide to make it vo lat il e. Inspite of this , many spectro metry. ESI was first conceived by Malcolm groups led by M. Shemya kin in USSR', K. Biemann Dole in the 1960's and by in corporatin g the in MIT, USA" and E. Lederer in France) were act ive ly tec hn ology that had become ava il abl e over the yea rs, in vo lved in research. John Fenn put ESI into use for biomolec ul e analysi s ]n J 970s, MS analys is of peptides progressed in the j 980'SI0. On the other hand MALOI uses a laser slowly, alth ough its potential was demonstrated by to desorb sampl e mol ecules from a solid or liqu id many groups for structure elucidation of modified matrix contain ing a hi ghl y UV -absorbing substance peptides. A rea l breakthrough came when Mi chael an d was developed by Franz Hillenk amp and Michael (Mickey) Barber discovered a new techn iqu e fo r Kara s". desorption and ionization of non-vo latil e organic Both ES I and MALOI fac ilit:lted adva ncements in compound s called Fast Atom Bombardment (FAB( the app lications of mass spectrometry in the fi eld s of 1n FAB , a beam of 3- 10 keY argon atoms was Ll sed to biology and med icine. In the j 990's, coupli ng of mass effec t desorption and ioni za ti on . Later it was found spectrometry with liquid chromatography syste ms that prima ry ions work just as we ll as atoms and this add ed a new dime nsion to the research in chemistry and bi oc hemistry. The limitati ons of mass *A uth or for correspondence spectro metry have yet to be defin ed as larger and 206 INDIAN J. BlOCHEM., BlOPHYS ., VOL. 39, AUGUST 2002 more complex molecules are being successfully production of ions fl~om collision with the analyte is characterized. Applications that were once stable. Even at a stable rate of ion production, inconceivable are In use today and include, ionization efficiency is low with EI techniques. In sequencing of peptides and proteins; studies of general, only one molecule in a thousand will undergo noncovalent complexes and immunological ionization. molecules; DNA sequencing; and the analysis of Ionization efficiency can be infl uenced by the intact viruses, to name a few. degree of interaction between the analyte and the electrons. The amount of interaction, and therefore the Introduction ionization efficiency, can be increased by increasing Mass spectrometry is one of the most important the anode current, increasing the width of the electron physical methods in analytical chemistry today beam, and increasing the sample pressure in the ion 2 bas ically because of its high sensitivit/ . The MS source. As always, there are practical limitations on performs primarily three functions; ionization of the extent to which one can increase each of these analyte molecules, resolve analyte molecules on the parameters. bas is of their mlz ratio and detection (Fig. 1). During the interaction of the energetic electron and the analyte molecule, a sufficient amount of energy is Ionization Methods transferred to the analyte to overcome its ionizati on The sarvple ions necessary for mass analysis are potential. The electron may transfer additional energy produced in the ion source. A good ionization method to the analyte, which may lead to the molecule should offer high ionization efficiency, should not be shedding two or even three electrons or to sensitive to the ion source conditions (e.g. , pressure or fragmentation of the initial molecula r ion. After temperature) or sample impurities, should produce ionization occurs, the ions are accelerated and then ions quickly, and should only produce one molecule focused through a potential field and sent on to the (structure) per ion (not isomeric mixtures). mass analyzer. 1. Electron Ionization (EI) A-B ---1~. [A-Bt + e' In EI the sample is vapourized usually by thermal [A-Bt ~ A + + B desorption. Once a sample is in the gas phase it passes into an electron impact ionization chamber. This small chamber contains a metal filament that is heated Electron impact is one of the most popular through a CUITent of 3-4 A to a temperature at which it ionization techniques for organic mass spectrometry. emits free electrons. The energy of the electrons is It is an easy technique that is very reproducible and controlled by the potential difference between the can be used for quantitati ve studies. Thi s method fil ament and the anode. tends to produce large amounts of fragments, whi ch The energy of the electrons is variable from 20-120 can either be a benefit or a di sadva ntage depending on e V (electron volts; 1 e V = 23 kcal), but reference the system. EI works best for molecul es under 400 Da spectra are typically obtained at 70 eV. At this energy because larger molecul es tend to be non- vo latil e and level, fragmentation patterns are reproducible and the decompose during vaporization. Analyte Mass Filter/ Molecules/ Ionization Source Analyzer Detector Sample + + + + +, + 00 + o + + + + t + +'"t"++ + + + ++ ++ + ++ 08~ ~ ++-It- + + ---+ 00 0 + + + ++ ... 00 + ++-f+ + +++ o 0 o + ++ + + + + + + + ~~Il~ ______ ~I~--~ ______ ~ Fi g. I- A schemati c di agram, showing th e bas ic design of a mass spectro meter. MAITHAL & MURALlDHAR : MASS SPECTROMETRY AND PROTEIN STRUCTURE 207 2. Chemical Ionization (CI) 3. Fast Atom Bombardment (FAB) CI is known as a soft ionization technique because The particle desorption methods were developed in the analyte is ionized without the transfer of excessive the late 1970's and early 1980's, superceding the energy to the resultant ions. Since the sample ions earlier field desorption method. The first particle have little excess internal energy, fragmentation is desorption method was plasma desorption, whi ch much less frequent in CI than in EI. CI is therefore made use of the 252Cf fission process to initiate useful for molecular structure and molecular weight desorption. The technique was fairly successful, but it studies. In addition, CI spectra can often reflect fine was soon overshadowed by the development of 4 14 I6 differences in structural isomers. CI is typically used FAB . ,IS and LSIMS , for the same types of samples as EI and will often The techniques of FAB and LSIMS invol ve the produce more abundant molecular ions than E11 3. bombardment of a solid analyte + matrix mixture by a > The CI ion source is essentially the same as the EI fast particle beam. The matrix is a small organic source. A similar metal filament is used to produce an species (glycerol or 3-nitrobenzyl alcohol, 3-NBA) electron beam, which then ionizes the reagent gas.
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