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̙33 *Struttura predefinita 0 '(     6H@P  )Predizione della struttura delle proteine* *`$  H  0޽h ? ̙33r "@(    0i0 ePredire la struttura secondaria 2    0@ MLe strutture secondarie sono determinate in primo luogo dalla struttura primaria che ha dei vincoli di disposizione nello spazio. Mediamente il 50% dei residui in una proteina si trovano in conformazione strutturata classica (alpha o beta) o altre conformazioni atipiche ma ugualmente strutturate. Le struttura beta-strand molto contesto dipendente, essendo influenzata da beta-strands vicini che originano dei foglietti, quindi molto difficile da predire. Le strutture alpha-elica sono strettamente dipendenti dal susseguirsi dei residui nella catena, quindi sono pi facili da predire. La struttura secondaria una caratteristica del BACKBONE delle proteine, non delle catene laterali. ,P 2h(2PhFVH  0޽h ? ̙33[  P(  j  0ip (Metodo statistico di Chou & Fasman e GOR) 2)F!0#!0%(-  0@ 0( Si basa sulla banca dati PDB Brookheaven, che raccoglie tutte le strutture proteiche note. 1- Osservazione della frequenza di ogni residuo in una struttura in ogni entry del database. 2 - Costruzione di una tabella di probabilit per ogni residuo in ogni struttura. 3 - Applicazione di un algoritmo di scorrimento a finestra per trovare i nuclei di strutturazione, prima alpha, poi beta, poi loops. 4 - Allungamento dei nuclei nelle due direzioni per trovare le regioni strutturate -2 I Zz 8Z  BXP J=> affidabilit: 64% -2 H  0޽h ? ̙33P `(  X  0A?`jH  0޽h ? ̙33 f^p(    00 w TAgadir 2|  0pN Non predice la struttura secondaria, ma analizza una sequenza alla ricerca di zone ad alta probabilit di formare una alfa elica. L approccio non statistico, ma TERMODINAMICO, consentendo una simulazione di strutturazione alfa in silicio  2 X  0A?\0 `X  0A?X  0A?.0^2  6opH  0޽h ? ̙33& `&X&^^ %(     0l`  _)Una possibile rete neurale (perceptrone)*(2*  0M z6MVLRST L FWENSA(7 2X  0 X  0 0`R  s * X  0 @pX  0 X2  0   X2  0 P X2  0  X  0 p R  s * X  0 0 ` X  0 X  0 @pX2  0 X2  0 X2  0 P X  0 X  0 @pX  0 X  0 PR  s * X2  0 0 X2  0 ` X2  0  R2  s * @ 0 X2  0p  X2  0p 0 X2  0p ` X2  0p  X2 ! 0p P X2 " 0p  X2 # 0p  X2 $ 0p @p X2 % 0p  X2 & 0p 0 R2 ' s * 00 X2 ( 0p @ p X2 ) 0p X2 * 0p 0 X2 + 0p ` X2 , 0p X2 - 0p P X2 . 0p X2 / 0p  X2 0 0p @p X2 1 0p  R2 2 s * p0 X2 3 0p  X2 4 0p  X2 5 0p @p X2 6 0p  X2 7 0p 0 X2 8 0p ` X2 9 0p  X2 : 0p P X2 ; 0p  X2 < 0p   = 0@0f  ^Pesi variabili definiti durante l apprendimento0 20RB > s *D  RB ? s *D p@ XB @ 0LD  XB A 0LD  LB B c $D` ` p LB C c $D` 0 ` p  D 00V ^ p() p() p(-)&0 2 RB E s *DP @RB F s *DP@ 0 @RB G s *DPP P @RB H s *DP @RB I s *DPp0@RB J s *DP@ K 0`p MSequenza input (13 residui)(2 L 00 0 OGruppi di input (21 elementi)(2 M 00$   ?Strato di input 2 N 0x(0`P @Strato di output 2R O s * @ R P s *  @ R Q s * R R s *  R S s *R T s * LB U c $D` ` p LB V c $D` P p LB W c $D` p LB X c $D` p ^2 Y 6o` @^2 Z 6oP` @` [ 0/  8 2" RB \ s *D`p RB ] s *D`P P RB ^ s *D`` H  0޽h ? ̙33 UM$(  $ $ 0L9i s%PHD (Profile network from HeiDelberg)& 2&% $ 0=@  r E basato sul concetto che se si multiallineano proteine simili, si ottengono delle conservazioni che rispettano la conservazione della struttura. 1 - La singola query viene mandata contro Swiss-Prot per trovare proteine simili 2 - Le proteine trovate vengono multiallineate 3 - Viene generato un profilo, che entra in una rete neurale (PHD) I risultati che si ottengono sono sottoposti ad una analisi statistica per valutare l attendibilit delle predizioni per ogni residuo. => affidabilit: dal 72% fino al 90%2 -2&(-2% H $ 0޽h ? ̙33 ?7((  (X ( 0A? d ( <A?? @p ( 0K0@w kLe due fasi principali di PHD 2H ( 0޽h ? ̙33 sk,(  , , 0Ti  UPSIPRED 2 , 0Y  NUtilizza un sistema composto da due reti neurali che analizzano i risultati della prima interazione di PSI-BLAST. 1 - Esecuzione di PSI-BLAST con la query desiderata 2 - Generazione di una PSSM (matrice posizionale di scoring) dai risultati della prima iterazione 3 - Predizione della struttura secondaria con una rete neurale opportunamente addestrata 4 - Una seconda rete neurale di correzione filtra il risultato e genera l output definitivo, valutando la confidenza per ogni residuo. 2X , 0A? @ `H , 0޽h ? ̙33 c[0(  0d 0 <A H?5 p 0 0xei P  SJPRED 2  0 0i |Lancia automaticamente molti programmi per la predizione della struttura secondaria e poi crea una sequenza consenso pesata.} 2} 0 0A ?0 !0H 0 0޽h ? ̙33 TL4(  4 4 0,ri n Database di strutture secondarie! 2! > 4 0v`  2DSSP (Kabsh & Sander): generato tramite il programma DSSP che ricostruisce le strutture secondarie da un file PDB in cui sono contenute informazioni tridimensionali, analizzando i ponti idrogeno. HSSP (Sander & Schneider): nasce dall allineamento di protine ad alta similarit, a cui viene fatto corrispondere un profilo di struttura secondaria comune. Esiste una entry hssp per ogni struttura proteica nota.0 2!0!0 4 6l0 P *L importanza di questi database sta nel fatto che molti metodi per la predizione li consultano per cercare delle similarit.}}H 4 0޽h ? ̙33/ 8o(  8X 8 0A ?` 8 0 @ ~E la banca dati delle strutture tridimensionali delle proteine@ 2@ 8 0X0   qSi effettuano per lo pi ricerche di tipo testuale, e il motore di ricerca indica quali sono le strutture trovater 2rX 8 0A ?- `0 X 8 0A ? &H 8 0޽h ? ̙33 <&(  < < 0Tip  iLe entries PDB: i file .pdb 2+ < 0ԛp\ Un file PDB un file di testo in cui sono riportate le coordinate di tutti gli atomi di una proteina, oltre a numerose altre annotazioni di varia natura.  2 < 00Pm HEADER ACYLPHOSPHATASE 08-NOV-96 2ACY TITLE ACYL-PHOSPHATASE (COMMON TYPE) FROM BOVINE TESTIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: ACYLPHOSPHATASE; COMPND 3 CHAIN: NULL; COMPND 4 SYNONYM: ACP; COMPND 5 EC: 3.6.1.7; COMPND 6 BIOLOGICAL_UNIT: MONOMER SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 ORGAN: TESTIS; SOURCE 5 CELLULAR_LOCATION: CYTOPLASM KEYWDS ACYLPHOSPHATASE, PHOSPHORIC MONOESTER HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR M.M.G.M.THUNNISSEN,P.NORDLUND 2>    <    ^ H < 0޽h ? ̙33 @9(  @ @ 00P6 jNel file PDB possono essere inclusi dati di struttura secondaria, ma non per questo che sono stati fattik 2k> @ 0h @ HELIX 1 H1 PHE 22 LYS 32 1 11 HELIX 2 H2 ALA 55 THR 67 1 13 SHEET 1 S1 5 HIS 74 VAL 85 0 SHEET 2 S1 5 LEU 6 LYS 16 -1 N ASP 10 O HIS 81 SHEET 3 S1 5 VAL 47 PRO 54 -1 N GLY 53 O ILE 7 SHEET 4 S1 5 VAL 36 ASN 41 -1 N VAL 36 O GLN 52 SHEET 5 S1 5 PHE 94 VAL 97 1 N VAL 97 O ASN 41 TURN 1 T1 PHE 22 THR 5 TYPE II' TURN 2 T2 PHE 14 VAL 17 TYPE IV TURN 3 T3 VAL 17 VAL 20 TYPE IV TURN 4 T4 THR 42 GLY 45 TYPE I TURN 5 T5 SER 70 SER 73 TYPE I  2 @ 0\@  !0 OManuale dei campi dei files PDB 2  @ 0p v zJEsistono delle sezioni precise del file in cui inserire certe informazioniK 2KH @ 0޽h ? ̙33 /'D(  D D 00P z _ ATOM 1 N ALA 1 13.196 6.710 0.033 1.00 80.57 N ATOM 2 CA ALA 1 11.875 6.755 -0.583 1.00 78.70 C ATOM 3 C ALA 1 10.858 6.436 0.487 1.00 77.39 C ATOM 4 O ALA 1 11.101 5.567 1.314 1.00 80.16 O ATOM 5 CB ALA 1 11.811 5.706 -1.691 1.00 79.51 C ATOM 6 N GLU 2 9.727 7.120 0.496 1.00 66.64 N ATOM 7 CA GLU 2 8.741 6.765 1.493 1.00 65.50 C ATOM 8 C GLU 2 7.398 6.494 0.835 1.00 65.06 C ATOM 9 O GLU 2 7.316 6.375 -0.396 1.00 62.92 O ATOM 10 CB GLU 2 8.748 7.578 2.788 1.00 66.75 C ATOM 11 CG GLU 2 9.232 6.756 3.974 1.00 67.60 C ATOM 12 CD GLU 2 9.572 7.604 5.177 1.00100.00 C ATOM 13 OE1 GLU 2 8.631 8.227 5.725 1.00100.00 O ATOM 14 OE2 GLU 2 10.759 7.641 5.577 1.00100.00 O ATOM 15 N GLY 3 6.346 6.331 1.627 1.00 57.60 N ATOM 16 CA GLY 3 5.059 6.045 1.024 1.00 54.68 C ATOM 17 C GLY 3 4.967 4.552 0.630 1.00 51.19 C` 2`  D 0 p 3Tag 2 D 0@p0` 7natomo 2 D 0`P0  : Tipo atomo 2  D 0@P ` 7Residuo 2 D 0   9 nresiduo 2  D 0L` ` < Coordinata X 2   D 0hP p < Coordinata Y 2   D 0@` < Coordinata Z 2   D 0 < Flessibilit 2 LB  D c $DLB  D c $DpLB D c $DLB D c $D` LB D c $DpLB D c $D`LB D c $DLB D c $D00LB D c $D LB D c $D @LB D c $D0 LB D c $D LB D c $D pLB D c $D p LB D c $D@ P LB D c $D0 LB D c $DLB D c $DpPpH D 0޽h ? ̙33 ?7 H(  Hf H 0  ` I programmi per la visualizzazione delle strutture tridimensionali delle proteine interpretano i files PDB posizianando  sfere di diametro adeguato nelle posizioni descritte dal files, posizionando i legami secondo i criteri imposti dal tipo di residuo (es. tutti i carboni alpha (CA) saranno legati insieme, ogni residuo avr i suoi atomi legati tra loro ecc.).l 2l H 0  UI programmi pi utilizzati per la visualizzazione tridimensionale delle proteine sonoV 2V< H 0 pp LRasMol : per la visualizzazione e l osservazione delle proteine Deep View  Swiss PDB Viewer: per una analisi dettagliata e per apportare modificazioni alla proteina 2!0!0A]H H 0޽h ? ̙33Y  0 L(  L L 00 w TRasMol 2u L 0\#R Presenta 2 finestre: la linea di comando e la parte grafica, in cui viene effetuato il rendering delle strutture. Si possono effettuare moltissime operazioni con il mouse senza scrivere nulla, ma molte altre non sono disponibili. 2X L 0A ?@X L 0A? X L 0A?m X L 0A?  X L 0A?@}PLB  L@ c $D  LB  L c $D ` LB  L c $D @ LB  L c $D  PH L 0޽h ? ̙33<    @P| (  P P 0/ ( 2 P 0,3 G UDisplay 2X P 0A?@X P 0A?0} X P 0A?# X P 0A?ctKX P 0A?`X  P 0A?  hX  P 0A? CbX  P 0A? `  P 09@ 9 wireframe 2   P 0=`  8backbone 2  P 0@  6sticks 2 P 0pD@0  9 spacefill 2  P 0Hp : ball&stick 2  P 0L`P  7ribbons 2 P 0O` ` 7strands 2 P 0R000P 7cartoon 2H P 0޽h ? ̙33 PT)(  T T 0Z`0 @ VCommands 2 X T 0A?  y  T 0(_ 0 Le selezioni si effettuano indicando o il numero dei residui o utilizzando dei gruppi predefiniti (es. select 10-20 seleziona i residui da 10 a 20, select 10,20 seleziona solo i residui 10 e 20, select arg seleziona tutte le arginine, select alpha seleziona tutte le alpha eliche). Combinando select, restrict e colour possibile mettere in rilievo particolari sezioni della molecola. 2 T 0e  Z*Si possono caricare degli  script , cio una lista di operazioni da svolgere in sequenza scritti in un unico file di testo con l opportuna sinatssi.  2H T 0޽h ? ̙33rXP+^$&+R?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~Root EntrydO)Pictures{Current UserSummaryInformation(PowerPoint Document(cDocumentSummaryInformation8