Download Foglio di stile per la tesi di dottorato

Foglio di stile per la tesi di dottorato in Scienze Chimiche e
Farmaceutiche
Formato carta: B5 (176 mm x 250 mm) si può stampare su qualsiasi
stampante, basta comprare o ritagliare da A4 la carta B5. Oppure chiedere
ad una stamperia.
Per la copertina usare cartoncino colore bianco perlaceo. Uguale per tutti.
Margini.
Superiore 25 mm. Destro e sinistro: 25 mm. Inferiore: 30 mm. Non lasciare
spazio per la cosiddetta Rilegatura. Numeri delle pagine posti in basso verso
il margine esterno. La copertina-frontespizio non va numerata e la tesi
comincia a p. 1 con l’Indice.
Caratteri. Usare caratteri Arial o Times New Roman.
Rientri: prima riga a capo usare rientro di 7mm.
Corpi e interlinea. Testo: corpo 11, interlinea singola. Infratesto (citazioni
ecc.): corpo 10, singola, rientro di 5 mm. Bibliografia: corpo 10, interlinea
singola.
Note. Corpo 10, interlinea singola.
Titoli dei capitoli corpo 12 grassetto e dei paragrafi corpo 11 grassetto.
Le abbreviazioni e gli acronimi devono comparire in una lista all’inizio del
capitolo nel quale compaiono.
Particolari tecnici:
È importante scrivere sempre l’unità di misura dei valori riportati nella tesi,
utilizzando il sistema internazionale di unità di misura.
Copertina: usare il templato presente sul sito del Dottorato SCF
Riscrivere sul modello scaricabile senza modificare la dimensione dei
caratteri e gli spazi (rendere omogeneo con il carattere scelto per la tesi).
Inserire n. del ciclo
Inserire il titolo ed il nome Candidata/o
Frontespizio: usare il templato presente sul sito del Dottorato SCF
Riscrivere sul modello scaricabile senza modificare la dimensione dei
caratteri e gli spazi (rendere omogeneo con il carattere scelto per la tesi).
Inserire n. del ciclo
Inserire il titolo ed il nome Candidata/o
Inserire Tutore e Cotutori.
Inserire Coordinatore del Dottorato
Esempio Arial:
affinity of the Fur protein for the Fur box DNA sequence does not require
iron, but iron availability regulates fur transcription in vivo so that other factors like the PerR protein may intervene 38.
It must be underlined that the five crystals structures of Fur proteins
present in the PDB (1MZB, 2FU4, 2W57, 2XIG, 4ETS), do not show any iron
bound, but show only zinc binding.
Of the three metal sites depicted in figure 2.5, one hosts a structural
Zn(II) ion bound to four Cys residues and is essential for the stabilization of
the tertiary structure of the protein and the dimerization domain. A second
metal binding site is located at the dimerization domain and involves a
HxD(X)mE(X)nH zinc binding motif which is considered a low affinity iron
binding site, not essential either for DNA binding and function of Fur 39. Mutagenesis and functional studies indicate that the third zinc binding site, connecting the DNA binding domain to the dimerization domain and comprising
the H(x)mE(x)mHxH(x)oE motif, is the high affinity Fe binding site responsible
for the sensing and regulatory functions of the protein 39,40.
Show picture of the site here
An analysis of the S. aureus proteome under conditions of iron deprivation and upon deletion of the fur gene, revealed global changes in gene expression and an overall switch from respiration to fermentation.
In addition to altering physiologic processes, bacterial pathogens also
modulate production of virulence factors upon changes in iron availability.
For example, biofilm formation occurs in response to iron limitation through
Fur-dependent mechanisms 41. In case of iron starvation Fur upregulates
several genes among which the membrane-bound ABC-type transporters
which are involved in heme acquisition by the cell 38.
Esempio Times New Roman:
affinity of the Fur protein for the Fur box DNA sequence does not require iron,
but iron availability regulates fur transcription in vivo so that other factors like the
PerR protein may intervene 38.
It must be underlined that the five crystals structures of Fur proteins present in
the PDB (1MZB, 2FU4, 2W57, 2XIG, 4ETS), do not show any iron bound, but
show only zinc binding.
Of the three metal sites depicted in figure 2.5, one hosts a structural Zn(II) ion
bound to four Cys residues and is essential for the stabilization of the tertiary structure of the protein and the dimerization domain. A second metal binding site is located at the dimerization domain and involves a HxD(X)mE(X)nH zinc binding motif
which is considered a low affinity iron binding site, not essential either for DNA
binding and function of Fur 39. Mutagenesis and functional studies indicate that the
third zinc binding site, connecting the DNA binding domain to the dimerization domain and comprising the H(x)mE(x)mHxH(x)oE motif, is the high affinity Fe binding
site responsible for the sensing and regulatory functions of the protein 39,40.
Show picture of the site here
An analysis of the S. aureus proteome under conditions of iron deprivation and
upon deletion of the fur gene, revealed global changes in gene expression and an
overall switch from respiration to fermentation.
In addition to altering physiologic processes, bacterial pathogens also modulate
production of virulence factors upon changes in iron availability. For example, biofilm formation occurs in response to iron limitation through Fur-dependent mechanisms 41. In case of iron starvation Fur upregulates several genes among which the
membrane-bound ABC-type transporters which are involved in heme acquisition by
the cell 38.