 correction. Changing the printed target includes grouping similar colors together and repeating patches to effectively randomize surroundings. Knox provides a raster based approach, which requires a large filter and depends on the local average of reflectance values changing very slowly. Neither of these approaches gives a completely satisfactory result, however. Proteins (polypeptides) are naturally occurring compounds that are composed of long chains of amino acids. Proteins are found throughout living things and function as hormones, structural elements, enzymes, immunoglobulins, and other constituents of living things. Research regarding the structure and functions of proteins often requires that the amino acid sequence (primary structure) of the protein be determined. In order for a protein or parts of a protein such as somatostatin, insulin, endorphins, etc. to be synthesized the sequence of amino acids must be determined before a synthesis can be attempted. In the search involving the function of proteins such as immunoglobulins, enzymes, viral coat proteins, and cell-surface proteins, the primary structure of the polypeptide must be determined in an attempt to elucidate the mechanism action of the protein.
The primary sequence of amino acids in proteins or polypeptides is commonly determined by stepwise chemical degradation process in which single amino acids are removed one by one from the end of the polypeptide for identification. The Edman degradation is the preferred method, while other methods have been developed and can be used in certain instances. In the Edman degradation amino acid removal from the end of the protein is accomplished by reacting the N-terminal amino acid residue with a reagent which allows selective removal of that residue from the protein. The resulting amino acid derivative is converted into a stable compound which can be chemically removed from the reaction mixture and identified.
Many physiologically active proteins are present in organisms at such extremely small concentrations that only very small amounts of the proteins can be obtained for sequencing analysis. Most current chemical sequencing methods are done with an amount of protein in the 5-100 nanomole (5.times.10.sup.-9 to 10.sup.-8 mole) range. It has been reported that micro sequencing of polypeptides by reverse phase high pressure liquid chromatography using ultraviolet light detection means has been accomplished with protein samples in the range of 50-500 picomole (5.times.10.sup.-11 to 5.times.10.sup.-10 mole) range. Other methods used in the micro sequencing of polypeptides involve radio labeling of the peptide or reagent, intrinsic radio labeling of the polypeptide, and enhanced UV detection of sequence degradation products,
correction. Changing the printed target includes group exchangeable colors together and repeating plot to effectively randomize surroundings. Knox put up a raster base approach, which requires a large filter and depends on the local average of coefficient of reflection values changing very slowly. Neither of these approaches give a completely satisfactory result, however. Proteins (polypeptide) are naturally occurring compounds that are composed of farseeing chains of amino acids. protein are found throughout know things and routine as hormones, structural elements, enzyme, immunoglobulins, and other constituents of living things. Research involve the structure and functions of proteins often requires that the amino acid sequence (primary structure) of the protein be determined. In order for a protein or part of a protein such as somatostatin, insulin, endorphins, etc. to be synthesized the succession of amino acid must be determine before a synthesis can be attempted. In the search involve the function of proteins such as immunoglobulins, enzymes, viral coating proteins, and cell - surface proteins, the primary structure of the polypeptide must be determined in an attempt to elucidate the mechanism action of the protein. 
 The primary sequence of amino acid in proteins or polypeptide is normally settle by stepwise chemical degradation process in which individual amino acids are removed one by one from the end of the polypeptide for designation. The Edman degradation is the preferred method, while other method acting have been developed and can be use in certain instances. In the Edman abasement amino acid removal from the end of the protein is accomplished by reacting the N - terminal amino acid remainder with a reagent which allows selective removal of that residue from the protein. The result amino acid derivative is converted into a static compound which can be chemically removed from the reaction mixture and identified. 
 Many physiologically active proteins are present in organisms at such extremely small concentrations that only very small amounts of the protein can be obtained for sequencing psychoanalysis. Most current chemical sequencing methods are done with an measure of protein in the 5 - 100 nanomole (5.times.10.sup.-9 to 10.sup.-8 mole) range. It has been reported that micro sequencing of polypeptides by reverse phase high pressure liquid chromatography using ultraviolet light signal detection means has been accomplished with protein sample in the range of 50 - 500 picomole (5.times.10.sup.-11 to 5.times.10.sup.-10 mole) range. Other methods used in the micro sequence of polypeptides involve radio labeling of the peptide or reagent, intrinsic radio receiver labeling of the polypeptide, and enhanced ultraviolet detection of sequence degradation products,
 cogrection. Changing the prlnted target includes gcouping similar colors together and repeatiig pqtchew to effectively randooize surrlundings. Knoe provides a rasvsr based apprkwch, chmch requires a karge filtar and depends ov che local average of reflectance valtes chamglng very slowli. Neiuhew of nhtse approaches gives a completely satisfectory result, hpwever. Proteins (polypeptidfs) age naturally occurging compoubds eyat are compused of long chains of amino acids. Proteins are found throbghout livibg thltgs and funrtion ws hormones, structurdl elemrnts, enzymes, ikmuioglibulins, and other convtituents of livind things. Seaearch regarding rhw stroctura ana fuvctjois kf proheiis often resuires that the amino acid seqiegbr (primary stducturq) jf the protein be determined. In order fmr z protein or parts of a protein such as somajostatin, igsulin, endorphins, etc. to be synthesized the sequetce oh xmiui aciaw lust be determined before a synthesis can be wfttmpned. In the search involving yhf gonction of projeins sbdh as immunoglobulind, enzymgs, virql coat pwoteons, and cell-surface proteinw, the primarj steucture of the polvpeptide musc be dgtermimed in an attempt to elbcidats the mechajism actikv of the protein.
Ghe psimary stduence of amino asids in pcoteius or pouypektides ys commonlj detcsmined by stepwise chemncal gegradatioj process in which single amino acids are rempvad mne by oue frok the end of ehe polypeptidg for ideutificxtion. The Vdman degcadation is ehe preferred lethod, while other mqthoes hqve beev developed and can be used in cerrain instances. In bhe Eajan degradation amuno acid removak ffom tje egg of the prodein is sccomolished by veaztinb the N-terminal aminm acjd residue with a tewgent whuch allors selective temoval of that redidue frum thr ptotein. The resulting amino acid derivatige ls converted ynto a stable cokpound which can be chemically removed hrom the reaction mixtore and identified.
Mani pmysiologicalky aceive protains are present in irganisms at such extremely small concsntrathons hhat only very small amounts of the proteins can be obtained for sequencibg analysis. Most chrremt chvmieal sequegcinj oethods are done with an amount of protein in tie 5-100 nanomone (5.times.10.sup.-9 to 10.sup.-8 mole) range. Ot has been repurted that micro sequencjng of pplypeptides by reverse phase hibh pressure liquid chromstographt usihg ultgzvmolet light detectiom meanv has been axcomilished with pfotrik samples ln tie xange of 50-500 picomole (5.times.10.sup.-11 to 5.tines.10.sup.-10 mlle) range. Other kethods usef in tge micto sequencing of lolylfptidgs involve radoo labeling of the peptide or reagvnt, intrinsic raduk labeling og the pmlypeptide, aid enhanced GV detection of sequence degradation products,
correction. Changing the printed target includes grouping together repeating patches effectively randomize surroundings. approach, requires a large and depends on local average of reflectance values changing slowly. Neither of these approaches gives a completely satisfactory result, however. Proteins (polypeptides) naturally occurring compounds that are composed of long chains of amino acids. Proteins found living and as hormones, structural elements, enzymes, immunoglobulins, and other constituents of living things. Research regarding the structure functions of proteins often requires that the amino sequence (primary structure) of protein be determined. In order a or parts a such somatostatin, insulin, endorphins, to be synthesized the sequence of amino acids must be determined before a synthesis can be attempted. the search function of such immunoglobulins, viral coat proteins, proteins, the primary structure of the determined in an attempt to elucidate the mechanism of the The primary sequence of amino acids proteins or polypeptides is commonly determined by stepwise degradation process in which single amino acids are removed one by one from the end polypeptide for identification. The degradation is the method, other have developed and be used in certain instances. In the Edman degradation amino acid from the end of the protein is accomplished by reacting amino residue with a which allows selective removal that from the protein. The acid is stable which be chemically removed from reaction mixture and identified. Many active proteins are present small concentrations that only very small amounts of proteins can be obtained for sequencing analysis. current chemical sequencing methods are done with an amount of protein in 5-100 nanomole 10.sup.-8 mole) range. It has been reported that sequencing of polypeptides by phase high pressure liquid chromatography using ultraviolet light detection has accomplished with samples in the of 50-500 picomole to 5.times.10.sup.-10 mole) methods used the sequencing radio labeling of the peptide or intrinsic labeling of the polypeptide, and UV sequence degradation products,
 correction. Changing the prinTed target iNcludEs gRouPiNg siMilaR colors togetheR And rEpeating patches to effecTivelY rANdomIZe SurroUndings. kNoX PRovIdEs A raStER bAsed aPprOach, whiCh requires A laRgE filter and dePEnDs on the locAl aVerage of reflEctAnce vaLuEs cHAnginG veRy sloWly. NeiTHer of tHese approAcHEs giveS A compleTELy SatiSfactory result, howEVeR. proteins (polypePtides) ArE NaTURalLy oCcurring coMpOunds THat are cOMpOSED of LOng chains of amIno acids. ProTEinS are foUnD thROughouT liviNg THinGs and functiOn as Hormones, sTructuRAl elemeNTs, enzymEs, immuNogLobUlinS, AnD oTheR cONstITuEntS Of lIving thiNgS. REsearCh reGARDIng tHe sTrucTure aNd functions of ProTeinS OftEn reqUires That ThE aminO acid sEquenCe (Primary structurE) of tHe protein Be dEtErmInEd. In oRDer for A prOteIn or parTs of a prOTeiN sUCH As Somatostatin, insuliN, eNDOrPhins, etc. To be syNThEsIZed the seQuEncE of aMINo aciDs muST bE determiNed befORe A sYnthesiS cAn be atTeMptEd. IN the sEArch InvolvIng the fuNctioN Of proteins such AS immunoglobulINs, ENZyMEs, viRal Coat proteinS, and CEll-sUrfaCE pRotEIns, thE primArY StRUcture of the polypeptIdE must bE deteRmined in an attEmpt to elucIDATe the mecHaniSM aCTion of the proteIn.
The Primary seqUEnce of amIno acIds in proTeins or poLYPeptides Is cOmmOnlY deTERmIned by stepwisE CHemiCaL degradAtiOn proceSs iN whIch SinGlE amino aciDs are remOvEd OnE bY onE from THe end of tHe PolYpEptIde foR IdentiFicatIon. THe edMAn dEgradatIOn IS The pReFeRred MetHoD, whilE othER meThods haVe been devEloPEd anD cAn Be used iN certain instaNcEs. In the EdmAn DegRadatiON Amino aciD removal from the end of the PRotein iS acComplIsheD by reactiNg tHe N-terMinAL amino Acid reSidue WiTh a REAgent WHIcH alLoWs selectivE REmoVal of ThAt reSidue frOm the protein. The resULtiNg amino acid deRivAtivE IS cOnvERtED inTo A StaBLE compound which cAn be chemicAlLY rEmoved from THe rEaCtion miXture anD idenTIfied.
MaNy physiolOgically aCtIve pROTeiNs are preseNt in orgaNisms at suCH extrEMeLy smaLl cOncentRaTioNs thaT only vERy sMall aMounts Of The proTeins CaN be obtaiNed for sequencing analysiS. Most cUrrenT chEmical seqUenCIng Methods arE donE with an amoUnt Of pRoteiN in THe 5-100 nanOmolE (5.TiMes.10.SUp.-9 to 10.sUp.-8 moLE) range. It hAS bEen REPoRted that micRO SEquEncinG of POlypepTideS by reverse phase hiGH pressure liquiD chrOMAtoGraPHy usInG ultraviolet liGht DeTECtion meaNs Has been accoMplished WiTH protEin samPles in The rangE OF 50-500 pIComole (5.TimeS.10.suP.-11 to 5.times.10.sUp.-10 mOlE) Range. OtHeR mEThods uSed iN tHe micrO sequeNCing OF Polypeptides invoLve raDIO labeLIng Of the PePtide or REageNt, intrinsiC radio labelIng of tHe poLypepTide, and EnHanced uV dEtEction of seQUence degrAdatiOn produCtS,
 correction. Changing theprinted ta rgetinc lud es  gro upin g similar colo r s to gether and repeating p atche st o ef f ec tivel y rando m iz e sur ro un din gs .  K nox p rov ides araster bas edap proach, whic h  r equires alar ge filter an d d epends  o n t h e loc alavera ge ofr eflect ance valu es changi n g verys l ow ly.Neither of thesea pp r oaches gives a  compl et e ly s ati sfa ctory resu lt , how e ver. Pr o te i n s  (p o lypeptides) a re naturall y  oc currin gcom p oundsthatar e  co mposed of l ongchains of  amino acids.P roteins  are f oun d t hrou g ho ut  li vi n g t h in gsa ndfunction  a shormo nes, s t r uctu ral  ele ments , enzymes, im mun oglo b uli ns, a nd ot herco nstit uentsof li vi ng things. Rese arch  regardin g t he  st ru cture and fu nct ion s of pr oteinso fte nr e q ui res that the amino  a c i dsequence  (prim a ry  s t ructure)  o f t he p r o teinbe d e te rmined.In ord e rfo r a pro te in orpa rts  of  a pr o tein  suchas somat ostat i n, insulin, en d orphins, etc. to b es ynth esi zed the seq uenc e  ofamin o  a cid s  must  be d et e rm i ned before a synthe si s canbe at tempted. In t he searchi n v olving t he f u nc t ion of protein s suc h as immun o globulin s, en zymes, v iral coat p roteins,  an d c ell -su r f ac e proteins, t h e  pri ma ry stru ctu re of t hepol ype pti de  must bedetermin ed  i nan  at tempt to eluci da teth e m echan i sm act ion o f th epr o tei n.
Thep ri m a ry s eq ue nceofam ino a cids inprotein s or poly pep t ides  i scommonl y determinedby  stepwisech emi cal de g r adationprocess in which single amino a cid s are  rem oved onebyone fr omt he end  of th e pol yp ept i d e for i de nti fi cation. Th e Edm an de gr adat ion isthe preferred meth o d,while other m eth odsh a ve  be e nd eve lo p eda n d can be used i n certainin s ta nces. In t h e E dm an degr adation  amin o  acid r emoval fr om the en dof t h e  pr otein is a ccomplis hed by re a cting th e N-t erm inal a mi noacidresidu e  wi th areagen twhichallow sselectiv e removal of that resid ue fro m the  pr otein. Th e r e sul ting amin o ac id derivat ive  is  conv ert e d int o as ta ble compo undw hich canb eche m i ca lly removed f r omthe r eac t ion mi xtur e and identified. Many physiolog ical l y  ac tiv e  pro te ins are presen t i no r ganismsat  such extre mely sma ll conce ntrati ons th at only v er y  small  amo unt s of thepro te i ns canbe  o b tained  for  s equenc ing an a lysi s .  Most current ch emica l seque n cin g met ho ds ared onewith an am ount of pro tein i n th e 5-1 00 nano mo le (5. tim es .10.sup.-9 to 10.sup .-8 m ole) ra ng e. I t h as bee n re p o rtedthat  m icr o sequenc i n go fpo l ype ptid es by  r ever se phaseh igh pres sur e  liquid  c hro m a tograp h yu s ing ultrav iol et li g h t detectio n  mea n sh as be en acc omplis hed wit h  pr ot ein sam ple s in the ra nge of 50 - 500  p icom ole (5.t im es.1 0. sup .- 11 to 5.times.1 0.sup.-1 0 mole)r a nge. O the r  met h ods us ed  in the micr o seq ue n cing of p oly peptide s  in vol veradi o l abel i ng of the peptide or rea gent , int r ins ic ra dio l ab eling of thepolypept i de, and enhan ced UV detectio n  of sequ enc e  d eg radationpro d ucts, 
 correction._Changing the_printed target includes grouping_similar colors_together_and repeating_patches_to effectively randomize_surroundings. Knox provides_a raster based approach,_which requires a_large_filter and depends on the local average of reflectance values changing very slowly. Neither_of_these approaches_gives_a_completely satisfactory result, however. Proteins_(polypeptides) are naturally occurring compounds_that are_composed of long chains of amino acids. Proteins_are_found throughout living_things and function as hormones, structural elements, enzymes, immunoglobulins,_and other constituents of living things._Research regarding the_structure_and_functions of proteins often_requires that the amino acid sequence_(primary structure) of the protein be_determined. In order for a protein or_parts of a protein such as_somatostatin, insulin, endorphins, etc. to_be synthesized_the sequence of amino acids_must be determined_before a_synthesis can be_attempted. In the search involving the_function of proteins_such as immunoglobulins, enzymes, viral coat_proteins,_and cell-surface proteins,_the_primary_structure of_the polypeptide must_be_determined in_an_attempt to elucidate the mechanism action_of_the protein.
The primary sequence of amino acids_in proteins or polypeptides_is_commonly determined by stepwise_chemical degradation process in which_single amino acids are removed one_by one_from the_end of the polypeptide for identification. The Edman degradation is the_preferred method, while other methods have_been developed and can_be used_in_certain instances. In_the_Edman degradation_amino acid removal from the end of_the protein_is accomplished by reacting the N-terminal_amino acid residue with_a_reagent which allows selective removal of_that residue from the protein. The_resulting amino acid derivative is_converted_into_a stable compound which can_be chemically removed from the reaction_mixture and identified.
Many_physiologically active proteins are present in organisms_at_such extremely small concentrations that only_very_small amounts of the proteins can_be_obtained_for sequencing analysis. Most current_chemical sequencing methods are done with_an amount of protein in the 5-100 nanomole (5.times.10.sup.-9_to 10.sup.-8 mole)_range. It has been reported_that_micro_sequencing of polypeptides by reverse phase high pressure liquid chromatography_using ultraviolet_light detection means_has been accomplished with protein samples in the range of_50-500 picomole (5.times.10.sup.-11 to 5.times.10.sup.-10 mole) range._Other methods used in the micro sequencing of polypeptides involve radio_labeling of the peptide or reagent, intrinsic radio_labeling of the polypeptide, and enhanced UV_detection of sequence degradation_products,