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Esistono 3 metodi principali di predizione:"O 2,(2{ {  6$O  B1 - Homology modelling: se si conoscono proteine simili con struttura nota 2  Fold recognition: se si va alla ricerca di strutture simili, cercando il folding migliore 3 - Ab initio: simulazioni di ripiegamento in silicio, molto complesse dato che si valutano tutte le possibili interazioni di tutti gli atomi con il solventeLe 2$2$I$$ eH  0޽h ? ̙33I    @ (    0pP s/Confronto con banche dati di sequenze proteiche0(20 0  0L$P 0 dAllineamento delle sequenze. E nota la struttura?3(23 3  0X$ 0 i%Predizione della struttura secondaria&(2& &  00 ` "  |8Homology modeling con le coordinate delle strutture note9(29 9  0pj NValutare l accuratezza della predizione( 2( (  0ԍ   M Threading (2    B<   UFoding ab initio (2   B܉@4 f  SRicerca di motivi LB  c $D00RB  s *D0 RB  s *D0 RB  s *D  0RB  s *D00 RB @ s *DPpp@RB  s *DP@@ RB  s *DP LB  c $D` LB  c $D  LB  c $D  LB  c $D  LB  c $D0  RB  s *D pLB  c $DPpPLB  c $D0PH  0޽h ? ̙33 ~vP\(  \ \ 0,i` `Homology modelling 2 \ 04^ j Assunzione di base: due proteine che presentano una identit del 30% circa, molto probabilmente avranno una struttura simile. Si va a valutare la r.m.s.d. (root mean square deviation) cio la distanza quadratica media tra gli atomi, generalmente i carboni alpha, ma si pu calcolare anche su tutti gli atomi. Minore il r.m.s.d. maggiore la similarit strutturale => stato osservato che proteine che condividono un identit di sequenza del 50% mantengono circa il 90% dei residui in posizioni conservaten 2(2 2 (~: H \ 0޽h ? ̙33. ``n(  `6 ` 0 L approccio all homology modeling abbastanza intuitivo, ma bene seguire delle considerazioni pratiche che possono essere definite Linee guida per costruire un buon modello: 1- Analizzare la struttura secondaria prima di quella tridimensionale, dato che se ci sono regioni fortemente random-coil, bene escluderle dalla modellazione (sono, per definizione, non modellabili). 2 - Identificare in banca dati una proteina a struttura nota che abbia una alta identit (> 50%) con la propria, o identit globale o identit locale. 3 - Allineare al meglio le due proteine. Rifinire l allineamento a mano, se necessario. Questa tappa critica, perch la modellazione verr fatta sulle proteine allineate.& 2+ H ` 0޽h ? ̙33P pd(  dX d 6l׸|0 4 - Cercare in banca dati il pi alto numero di proteine simili tra loro e identificare dopo il multiallineamento le regioni di struttura secondaria conservate (in genere se ci sono dal multiallineamento si vede). Si costruisce cos un pre-modello. 5 - Modellare per prima cosa le regioni altamente variabili (in genere i loops) che connettono regioni a struttura secondaria definita. Esistono database anche dei loops (tutti i loops osservati), quindi non si modella a caso, ma si cerca la struttura di un loop gi presente. Se non c , o se ce ne sono pi di uno compatibile, osservare le regioni pre-loop e post-loop. 6 - Modellare le catene laterali sulla base delle catene della proteina nota. Esistono per questo delle librerie di ROTAMERI, cio isomeri delle catene laterali con angoli di torsione adeguati alle torsioni del backbone. &P 2 X PH d 0޽h ? ̙33z *"l(  l l 0|P  f$7  Risolvere, se possibile, i problemi relativi alle collisioni dei vari atomi, o manualmente o con programmi che indicano l energia minima delle strutture. Alla fine gli atomi di una proteina non dovranno collidere, e la proteina dovr essere alla minor energia possibile. 2  l 0 0p  T Nonostante ci siano delle regole abbastanza precise, l homology modelling molto complesso e richiede un grande lavoro e molto tempo.(2 H l 0޽h ? ̙33X p(  p p 0ip jFold recognition (threading) 2n p 0@g Il concetto di fondo che: le proteine presenti in natura hanno un numero finito di strutture possibili, o almeno un numero finito di topologie (<1000). D 2(2 2  p 0\ڸ `O ZDavid Heisenberg ha sviluppato il metodo dei profili 1D-3D. Si tratta di catalogare tutti i FOLD possibli in termini di INTORNO per ogni posizione di ogni fold. L intorno definito con 1 - Struttura secondaria. 2 - Accessibilit al solvente. 3 - Tipo di residui circostanti (polari, apolari). Ogni fold viene descritto come una sequenza (1D) di simboli associati a frequenze di ritrovamento in una data struttura 0 2- r H p 0޽h ? ̙33 d\(    0 `a \E possibile cos confrontare una sequenza proteica allineandola con tutti i possibili profili di tutti i fold conosciuti, ricavando un punteggio che valuti il best fitting della sequenza. Facendo cos si in grado di identificare strutture di proteine anche molto divergenti tra loro, al punto di non essere riconosciute da nessun programma di allineamento o di similarity search. Un esempio tipico l individuazione della struttura di proteine che hanno la stessa funzione a causa di una evoluzione convergente: originandosi da geni diversi non correlati, la sequenza (sia aminoacidica, sia nucleotidica) saranno molto diverse, ma la struttura terziaria, almeno nell intorno del sito catalitico, deve essere costante per garantire una stessa funzionalit :(2 A H  0޽h ? ̙33 $(    0ݸi _Metodo di Rosetta 2  0I  |Messo a punto dal gruppo di David Baker, non si basa sulle banche dati di fold di riferimento predeterminati, ma segue tre fasi empiriche con alta capacit predittiva: 1 - Divide la sequenza primaria in gruppi (da 3 a 9) residui, ed effettua una ricerca tra le proteine a struttura nota. Si generano cos, per ogni frammento, una serie di strutture 3D possibili. 2 - Tutte le possibili combinazioni di strutture 3D locali vengono generate, e considerate inizialmente ugualmente possibili. 3 - Si applicano funzioni di scoring, di minima energia, di comparazione, per assegnare dei punteggi che indicano la qualit di ogni struttura. } 2} }  0Kp v ]=> tra i sistemi di fold recognition, quello che ha ottenuto i migliori risultati al CASP. ^ 2^ ^H  0޽h ? ̙33 qi(    0> P RCASP 2P  0`@r E una gara tra i gruppi che sviluppano metodiche di modeling 3D e 2D che si basa sulla predizione delle strutture data una serie di sequenze proteica e basta. I modelli migliori vengono valutati sulla base& 21 X  0A ?@pg  04` bdella loro somiglianza con le strutture 3D ottenute sperimentalmente ma tenute segrete fino al giorno delle presentazioni. Vengono valutati separatamente i tre diversi modi di fare predizioni di struttura. Il CASP permette di valutare quale il miglior metodo per generare un modello proteico, tenendo aggiornati tutti sui progressi dei vari gruppi di ricerca e garantendo cos agli utenti finali, per esempio voi, di utilizzare la tecnica predittiva pi aggiornata e pi affidabile. Inoltre, essendo una competizione, stimola la ricerca e la continua innovazione alla ricerca del metodo predittivo perfetto c 2c cK  6 0@ CCritical Assessment of techniques for protein Structure Prediction tD$   DH  0޽h ? ̙33 ^(    0<ø90 ^Swiss-PDB Viewer 2X  0A?  0|0P` :E molto pi complesso e con una interfaccia meno immediata di RasMol, ma ha delle potenzialit enormi da un punto di vista di analisi, modellazione e rendering 3D delle proteine. Vengono implementati tutti i metodi per 1 - homology modeling 2 - structure alignment 3 - manual refining delle strutture 4 - calcolo delle energie minime 5 - introduzione delle mutazioni strutturali} 2} }^2  6op@H  0޽h ? ̙33w '(    0``P q _Possiede 2 finestre di lavoro principali: 1 - Control panel: dal quale si guidano tutte le impostazioni grafiche di visualizzazione e di colorazione 2 - Graphic window: nella quale viene visualizzata la struttura della proteina 8 2. lE X  0A? 0X  0A?P H  0޽h ? ̙33 C; (  6  0XQ  Imparare come lavorare con il control panel , per la parte di visualizzazione, la cosa pi importante, dato che non intuitivo & 2q X  0A? P  0Vp asu quale layer si sta lavorando 2  X  0A?/PX  0A ?/  0[p0 alayer visibile e/o layer mobile 2  X  0A!? I  0_`pP2  gruppo, inteso come residuo, quello corrente in grassetto, quelli selezionati sono rossi. Nella colonna viene riportata la struttura secondaria ricavata dal file PDB 2 X  0A"?@ n  0d p :show: l elemento selezionato visibile. side: la sua catena laterale visibile. labl: la sua atichetta (group) visibile.} 2} }H  0޽h ? ̙33 UM (  X  0A'?Q ` UX  0A#?X  0A$?Pp{  0`m controllo della superficie, che va prima calcolata: Van der Waals: una sfera punteggiata Superficie molecolare: renderizzabile Superficie accessibile: al solventeJ 24  X  0A%? _ X  0A&?    0Ģ` `  ]Superficie di Van der Waals 2   00 WSuperficie molecolare 2   0 0 f$Superficie molecoare (rendered view)% 2% %H  0޽h ? ̙33. "n(  2  Zvd @ 2  Zvd @ @ 2  Zvd @P  2  Zvd @ P 2  Zvd @@  2  Zvd @ Pp 2  Zvd @ p@2  Zvd @ ` `2  Zvd @ 0 2  Zvd @ P 2  Zvd @ p ` 2  Zvd @ @ 2  Zvd @P @ 2  Zvd @ @0 2  Zvd @ 0 2  Zvd @ `@ X2  0 RB  s *D``   BC:DEFPo44: 'lP1^ 3HLX|*AVeR9  \ "  Z p P p`*:(R*jp:   x| %(@                  P    lB[CDEFH3o..$aJpRNK9`Og"u?   D  d m  r]  } ; '_AYc9Ug2E#*6[3!$@               Sc% X2  0@ 0   08i!0 JMolecola 2    0m!  ]Superficie di Van der Waals 2   0l!  WSuperficie molecolare 2   0t!0 P XSuperficie accessibile 2 LB @ c $D PLB  c $D0` LB  c $D p  w ! 0|x!dP La superficie accessibile va vista come la linea che percorrerebbe il centro di una una sfera di solvente a raggio fissato (es. 1.4), quindi uguale alla superficie molecolare + 1.4.0 21    " 0~!0  Y r = 1.4" 2" H  0޽h ? ̙33 z (  X  0A(?p  0! XRibn: controllo dei  nastri (ribbons): il gruppo selezionato avr il suo ribbon visualizzato, se sono accesi e configurati i ribbons. Visualizzazioni: si configurano tutti i tipi di visualizzazione, definendo le propriet per ognuno dei diversi tipi.0 2f X  0A)? pX  0A*?Gp   0!P  XLa configurazione delle visualizzazioni e il fatto che esse siano visibili oppure no non sono dipendenti nel control panel: questo permette di configurare tutto all inizio e poi decidere cosa e come visualizzarlo. Ogni tipo elemento pu essere visualizzato contemporaneamente nella finestra grafica.- 2- -H  0޽h ? ̙33@ 0(  R  s *A+&   0ԛ!0  0La gestione dei colori una cosa particolarmente importante e complicata in Swiss PDB Viewer: dato che molte cose possono essere visualizzate contemporaneamente, tramite la colonna colori si impostano tutte una per volta. Ogni residuo ha il suo colore, ma il colore che si sceglie subordinato alla struttura che ho selezionato prima con la scelta delle visualizzazioni. Per selezionare tutta la colonna si usa il tasto destro del mouse oppure si trascina una selezione su tutta la colonna.  2 V  0!p `B IMPORTANTE: se si seleziona un altra visualizzazione, sar visibile la colorazione per quella visualizazione soltanto. Tutte le altre, anche se non sono visibili, rimangono, per.  2 H  0޽h ? ̙33B @ (  X  0A? \  0\!  p.Porta la proteina al centro, dovunque si trovi/ 2/ /  00!D  0  BLega il bottone sinistro del mouse alla traslazione della proteinaC 2C C  0! P   n,Lega il bottone sinistro del mouse allo zoom- 2- -  0!P"  @Lega il bottone sinistro del mouse alla rotazione della proteinaA 2A A  0!P  b Visualizza il testo nel file PDB! 2! !LB  c $D  pLB  c $DP0 LB  c $Dp ` LB  c $D  LB  c $DPH  0޽h ? ̙33  S K P (  X  0A?0(  0P!` YDistanza tra due atomi  2   0!@ VAngolo tra due atomi 2   00!  LAngoli diedri tra i legami dell atomo ' 2' '  0 !`  K Etichetta 2  l  0!P `T  Seleziona atomi compresi in un raggio r dall atomo selezionato e viene chiesto che operazione faref 2f f  0!@ WPosiziona al centro(2   0$!`P L Mai capito 2  LB  c $D`LB  c $D` LB  c $D` LB  c $D0 ` LB  c $D0LB  c $D`p`LB  c $D`X  0A?   0l!   >Le informazioni richieste vengono visualizzate sotto i bottoni? 2? ?LB  c $D p LB  c $D0 LB  c $D LB @ c $D X  0A?p 0JH  0޽h ? ̙33 nf`(  X  0A?yX  0A?X  0A?/y LB  c $DLB  c $D X  0A? LB  c $D  0!) WSelezioni predefinite 2   0p!  TColori predefiniti 2   0!  SPersonalizzazione 2 2  B!o) : 2  B!o  : 2  B!o y : H  0޽h ? ̙33o  (  X  0A ?P- X  0A?Cy X  0A ?c`LB  c $D`LB  c $DP `LB @ c $D` P  00 ZLa superficie molecolare e altre cose vanno calcolar eprima di pterle usare (es. colorare)[ 2[ [W  0   Visto che il programma non dedicato esclusivamente alla parte grafica, come RasMol, il rendering pu essere acceso o spento per risparmiare risorse per il calcolo. Per vedere i ribbons tridimensionali, le superfici ed altro, il rendering deve essere acceso a mano o con quegli acceleratori. Se il rendering spento, solo la visualizzazione wireframe disponibile, MA QUI NON SI CHIAMA WIREFRAME, non hanno un nome le visualizzazioni! 2 H  0޽h ? ̙33rl Pb,83n:BHH(@OdWP]1[f?loYx<^S. <ZOh+'0H `h  Presentazione di PowerPointMatramaMatrama24rMicrosoft PowerPointrPo@R@` 2@@a4BG<g  g& &&#TNPP2OMi & TNPP &&TNPP    - "-- !-- "-&G& - &Gy& --I -- @Times New Roman- .'2 :Predire la struttura       . .2 :D terziaria   .--P0-- @Times New Roman- .g2 s:@E di gran lunga la predizione pi complessa che si possa fare su               . .2 : una proteina.   . .H2 +Esistono 3 metodi principali di predizione:            .---- @Times New Roman- . 2 $"1  . . 2 $F-. .%2 $bHomology modelling: #&  &  .@Times New Roman- .R2 ]R2se si conoscono proteine simili con struttura nota             .@Times New Roman- . 2 "2  . . 2 F. ."2 jFold recognition:      .@Times New Roman- .g2 R@se si va alla ricerca di strutture simili, cercando il folding m               . .2 Jigliore   .@Times New Roman- . 2 "3  . . 2 F-. .2 b Ab initio: "    .@Times New Roman- .g2 DR@simulazioni di ripiegamento in silicio, molto complesse dato che                . .^2 mR:si valutano tutte le possibili interazioni di tutti gli at                  . .2 m omi con il   . .2 Rsolvente   .--"System-&TNPP &Z՜.+,0h    Presentazione su schermoP Casa Miaion83_ Times New RomanStruttura predefinitaPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPoint Caratteri utilizzatiModello strutturaTitoli diapositive_MatramMatram  !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#%&'()*+-./0123>Root EntrydO)PicturespCurrent User,SummaryInformation(xPowerPoint Document((DocumentSummaryInformation8$