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Viene richiesta soltanto una (o pi) sequenze di riferimento su cui modellare la struttura. Le procedure sono semplici, ma la validazione complessa come tutti gli altri tipi di predizione strutturale. Costruire un modello semplice. Rifinire un modello complesso. Validare un modello molto complesso, e serve una parte sperimentale. Per l homology modeling sono disponibili dei server dedicati all automazione delle operazioni di base (raccolta degli omologhi strutturali, allineamenti, validazioni ecc.)>:(2(2(2xl  1 H  0޽h ? ̙33 @>(    6A?< !0x  0@ ] E il server pi utilizzato, permette di tracciare tutte le operazioni che svolge e di impostare alcuni parametri importanti per il risultato finale. Vi si accede on-line, oppure interfacciato con Swiss PDB Viewer che lancia le procedure base e poi permette di perfezionare i risultati grazie ai suoi strumenti di modeling.(H(2&n>eH  0޽h ? ̙33F P(  X  0A?`  00 `@ h8La versione on-line suddivide il lavoro in cinque tappe principali: l utente pu posizionarsi in varie posizioni a seconda delle informazioni di cui dispone 2X  0A?pP0= X  0A?j ^2  6oH  0޽h ? ̙33 `(    0d'0w tRicerca dei templati possibili 2    0+;   Viene utilizzato il programma BLASTP2 per cercare similarit di sequenza primaria contro la banca dati ExNRL-3D, contenente le controparti adattate per la ricerca blast delle di tutte le proteine contenute nella banca dati ExPDB, forma non ridondante e non annotata generata della PDB. Visto che si utilizza BLAST, possono uscire pi templati adatti perch : 1 - Esistono effettivamente pi templati che hanno un alta similarit globale con la sequenza di interesse. 2 - I templati trovati corrispondono a zone diverse della sequenza di interesse, che possiedono alte similarit locali. F(2= 2g77j 0 O +CH  0޽h ? ̙33= p }(    0/` sRicerca dei migliori templati 2  0@@ ` <Vengono scelti tra tutti i modelli possibili quelli che hanno identit maggiore del 25% da allineamento pairwise struttura/sequenza e viene progettata la modellazione di tratti di sequenza lunghi pi di 20 residui.(2,hAX  0A?p #X  0A?` r |  6LG4  Grazie a questa operazione di ottimizzazione, vengono applicati i criteri dell homology modelling.c 2cI^2  6op P ^2   6o `P    0L  V&Due diversi domini per la modellazione' 2'H  0޽h ? ̙33 V(    0T qCostruzione dei pre-modelli 2   0pX  Viene lanciato il programma ProModII su tutti i templati trovati. La sequenza delle operazioni svolte da ProModII offre, per ogni templato, un modello strutturale ottimizzato della sequenza di interesse grazie agli allineamenti strutturali generati dal programma SIM. (2>  0X  0A?PaH  0޽h ? ̙33  ~ v  (    0c` NOttimizzazioni energetiche 2  0g `l 2Viene applicato Gromos96 ad ogni struttura modellata, per valutare l affidabilit energetica del modello e per effettuarne la minimizzazione entergetica. 2 X  0A?pi^2  6o ^2  6o P ^2  6oP  ^2  6o `    <oT DConversione formati   0r ` KCostruzione della topologia   <$vKV E GAggiunta degli idrogeni  0y@* NCalcoli di dinamica molecolareRB  s *Do0RB  s *Do`  RB @ s *Do0p RB @ s *Do0@ H  0޽h ? ̙33  (      00 'yAlla fine viene prodotto un file contenente tutte le strutture utilizzate per la modellazione e la struttura incognita modellata (TARGET), con tutti gli allineamenti strutturali. I risultati, compresa tutta la lista delle operazioni svolte dai vari programmi, vengono spediti via e mail e la struttura modellata si presenta come un progetto di Swiss PDB Viewer (nomefile.pdb). :z(2\PXX   0A ?@ H   0޽h ? ̙33 "(    0p  La struttura modellata contiene anche informazioni riguardanti la confidenza della predizione. Nell ultima colonna dei record ATOM del file PDB in genere sono contenuti i dati sulla mobilit dell atomo ottenuta dai dati NMR o di cristallografia: In questo caso il B-FACTOR non sperimentale ma ottenuto da un analisi statistica della struttura modellata con tutti i templati disponibili ed legato a 1 - Numero dei templati utilizzati per il modelling 2 - Deviazione di posizione del modello dai templati 3 - Distance trap (la soglia di distanza considerata di inattendibilit)X(2 2B tq *  , #H  0޽h ? ̙33  _(  X  0A ? r^2  6o   0ܢ@ 8Se sono noti degli allineamneti rifiniti a mano e sicuramente attendibili possibile utilizzare l interfaccia con l allineamento anziche il first approach. 2> b   0p0(  0Viene chiesto di incollare un allineamento, che deve contenere al suo interno la proteina da modellare e anche la struttura o le strutture di riferimento. In questo modo la modellazione parte da uno step successivo rispetto prima, saltando tutta la prima parte di ricerca dei templati e di allineamento. 1 21,T X  0A ?8 0X  0A ? ? ^2   6o0 P`P    0P   oDa cercare nel database ExPDB 2RB   s *Do PH  0޽h ? ̙33  V N (  X  0A ? r^2  6o0  0@ Dopo un primo modelling, possibile perfezionare a mano l allineamento strutturale e salvarlo come progetto swiss-model in Swiss PDB Viewer. (2P V   0ؿr  Questo modo il pi raffinato e il pi  pericoloso : si utilizzano solo gli strumenti di refining del server Swiss-Model, ma il modello sostenzialmente gi fatto, quindi se sbagliato (es. allineamento non corretto, templati sbagliati ecc.) rimarr sbagliato!  (2 PZ  A%  0P  x6Da Swiss PDB Viewer possibile lanciare direttamente una richiesta di modellazione ottimizzata, data che l ottimizzazione possibilie con gli strumenti di modellazione fine del programma. Anche in Optimize mode i risultati vengono spediti via e-mail, e vanno riaperti in seguito.  2 H  0޽h ? ̙33u %(    0@ ,Utilizzare Swiss PDB Viewer per il modelling- 2->    0  P IIn generale, Swiss PDB Viewer viene considerato un programma per valurate la qualit di un modello strutturale e per il manual refining delle strutture. In effetti per possibile iniziare e portate a termine un progetto di modellazione interamente, senza utilizzare la versione on-line di SWISS-MODEL. In alternativa, si effettua il modeling con il server e poi si apre il progetto che arriva via e-mail e si corregge a mano. (2b # . UX  0A ? ^2  6o H  0޽h ? ̙33-  m(      0i@ SValutare la qualit del modello 2 z   0 81 - Osservare il r.m.s.d. tra modello e templato. 2 - Colorare tutto in base al B-factor (se c ). 3 - Osservare il plot di Ramachandran. 4 - Selezionare gli amino acidi in collisione tra loro. 5 - Selezionare gli amino acidi in collisione con il backbone. 6 - Selezionare gli amino acidi con legami idrogeno impropri. 7 - Osservare le polarit dei residui esposti e sepolti. 8 - Calcolare l energia libera.  2( ! 36 5 1H   0޽h ? ̙33; ${(  $ $ 0  W#Modificare la struttura del modello$ 2$X $ 0A?PpX $ 0A?@P  $ 0$PX rPermette di modificare un residuo con un altro, ma anche di cambiare il ROTAMERO della catena laterale: in natura infatti ogni residuo presenta la catena laterale in un certo numero finito di disposizioni (rotameri) archiviate in una libreria apposita.8 2HfA' $ 08P/ Permette di modificare tutti gli angoli di legame del residuo selezionato: se si cambiano gli angoli phi e psi naturalmente si sposta anche il backbone della proteina e bisogna decidere se pu spostarsi l N o il C terminale. Per evitare gli spostamenti delle estremit si pu rompere temporaneamente il legame peptidico, per poi effettuare le modifiche e la nuova ligazione. y 2ybe 3g :H $ 0޽h ? ̙33 >6<(  < < 00Pw BPerfezionamento dell allineamento" 2"!X < 0A?1 x> < 0tPC  ~La finestra Alignment mostra l allineamento strutturale come stato generato dal server di modelling. E possibile modificare l allineamento selezionando il residuo da spostere e: spacebar/del: inserimento/rimozione di un gap freccia dx/sx: spostamento del residuo Ogni modifica si riflette anche sulla struttura. Il plot riguarda la  threading energy , cio un valore che indica quanto adatto il residuo a stare in quell intorno di residui.2 2W -2 -2 H < 0޽h ? ̙33  ,7(  ,X , 0A?  , 0 0 w _Ramachandran plot 2 p , 0$ 0W  dGiallo: aree permesse Blu: aree limite Quadrati: glicine Crocette: altri residuie 2et    , 0+ PPer ogni residui vengono plottati i rispettivi psi su phi: solo certe combinazioni sono permesse. Inoltre possibile cambiare gli angoli trascinandoli nel grafico. Il backbone della proteina cambia!  2P  o  , 01  HLe glicine vanno trattate a parte parlando di angoli permessi: l amino acido cos piccolo che non ha in pratica angoli vietati... 2 H , 0޽h ? ̙33 00Z(  0 0 00;iP r$Riorientamento delle catene laterali% 2% 0 0?p0v DE possibile riorientare le catene laterali in termini di rotameri dal menu Tools -> Fit Selected SidechainsP !  X 0 0A?b 0 0 Epl  =Quick and Dirty: mette il rotamero a minor score Exaustive search: prova tutti gli angoli possibili Simulated annealing: non funziona B 2"$P   +  0 0M p  >Lo score (clash score) di uno spostamento calcolato secondo:? 2? 0 0 04R 0p ? 4 x numero di scontri tra atomi del legame peptidico + 3 x numero di scontri con gli ossigeni del backbone + 2 x numero di scontri delle catene laterali - numero di idrogeni - 4 x numero di ponti disolfuro formati  2,. - nH 0 0޽h ? ̙33 @8;4(  4 4 0t[@ BPonti idrogeno 2 4 0_@0 :Possono essere  facilmente localizzati osservando i tipi di atomi e le distanze tra di essi. Di default viene assegnato un ponte idrogeno se un donatore e un accettore si trovano tra 1.2 e 2.76 e con un angolo di 90 se non c l idrogeno, tra 2.35 e 3.2 e 120 se c l idrogeno. 2[ > FX2 4 00`  4 0i`0  1D 2X2 4 0`  4 0m00  1H 2X2 4 0 `   4 0oP 0  1A 2XB  4 0D`XB  4 0DX2  4 0` `   4 0 8X 8 0A?yX 8 0A?n X 8 0A? 0+u  8 0迸 :  v*Threading energy Campi di forza Deviazioni+ 2+^2  8 6o 0o RB  8@ s *Do p0  8 0@ŸJP0P Cliccando sopra tutti i possibili loops generati vengono ordinati in base al criterio di scelta fatto, permettendo la scelta del loop. 2 ~RB  8 s *DoP ,  RB  8 s *Do   RB 8 s *Do 0  H 8 0޽h ? ̙33r` A =@#'/ 7>;EHaO X7glmXE|Df|u PZOh+'0h `h  Presentazione di PowerPointMatramaMatrama32rMicrosoft PowerPointrPo@ H@` 2@ +4BGZg   g& &&#TNPP2OMi & TNPP &&TNPP    - "-- !-- "-&G& - &Gy& --IP-- @Times New Roman- ."2 :ZHomology modelling   .--\ -- @Times New Roman- .$2 *Lomology modeling    . .H2 Y+delle proteine il tipo di predizione di             . .g2 *@struttura terziaria pi semplice ed affidabile. Viene richiesta                 . .2 1 soltanto    . .g2 *@una (o pi) sequenze di riferimento su cui modellare la struttur                 . .2 Ua. Le   . .62 *procedure sono semplici, ma la          . .2  validazione    . .*2 j complessa come tutti       . .F2 **gli altri tipi di predizione strutturale.             .@Symbol- . 2 R*.@Times New Roman- .72 RR Costruire un modello semplice.       .@Symbol- . 2 *.@Times New Roman- .72 R Rifinire un modello complesso.      .@Symbol- . 2 *.@Times New Roman- .2 R Validare   . .N2 /un modello molto complesso, e serve una parte        . .2 Z sperimentale.    . . 2 %*Per  . .%2 %jlhomology modeling   . .?2 %%sono disponibili dei server dedicati          . .g2 K*@allautomazione delle operazioni di base (raccolta degli omologh                . . 2 Ki . .02 q*strutturali, allineamenti,       . .2 qd validazioni    . .2 qecc.) .--"System-&TNPP &Z՜.+,D՜.+,T    Presentazione su schermo. Casa Miaionf Times New RomanSymbolStruttura predefinitaPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPointPresentazione di PowerPoint Caratteri utilizzatiModello strutturaTitoli diapositive 8@ _PID_HLINKSA0http://www.expasy.org/swissmod/SWISS-MODEL.html_!MatramMatram  !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~     !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijkmnopqrstuvxyz{|}~Root EntrydO)PicturesCurrent UserSummaryInformation(lPowerPoint Document( DocumentSummaryInformation8w