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Pregled bibliografske jedinice broj: 306793

Koreliranje oblika površine i hidrofobnosti proteina korištenjem razvoja u kugline funkcije


Dokmanić, Ivan; Šikić, Mile; Tomić, Sanja
Koreliranje oblika površine i hidrofobnosti proteina korištenjem razvoja u kugline funkcije // Book of abstracts, The 2nd Opatija Meeting on Computational Solutions in the Life Sciences / Babić, Darko ; Došlić, Nađa ; Smith, David ; Tomić, Sanja ; Vlahoviček, Kristian (ur.).
Zagreb: Ruđer Bošković Institute, 2007. str. 69-69 (poster, međunarodna recenzija, sažetak, znanstveni)


Naslov
Koreliranje oblika površine i hidrofobnosti proteina korištenjem razvoja u kugline funkcije
(Correlating protein surface shape and hydrophobicity using spherical harmonical expansions)

Autori
Dokmanić, Ivan ; Šikić, Mile ; Tomić, Sanja

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Book of abstracts, The 2nd Opatija Meeting on Computational Solutions in the Life Sciences / Babić, Darko ; Došlić, Nađa ; Smith, David ; Tomić, Sanja ; Vlahoviček, Kristian - Zagreb : Ruđer Bošković Institute, 2007, 69-69

ISBN
978-953-6690-69-5

Skup
The 2nd Opatija Meeting on Computational Solutions in the Life Sciences

Mjesto i datum
Opatija, Hrvatska, 4-9.9.2007.

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
Protein ; Docking ; Spherical Harmonics ; Hydrophobicity ; Shape Correlation

Sažetak
Ability to efficiently match different surface properties is essential for the search phase of a docking procedure. Following the earlier work [1, 2] we implemented a docking search algorithm that uses expansions of surface properties - shape and hydrophobicity - into series of spherical harmonics and special radial functions. Correlation between two surfaces is thereafter performed using the expansion coefficients. For the docking search it is necessary to transform 3 rotational and 3 translational degrees of freedom into 5 rotational and 1 translational. Rotations are performed by applying the Wigner rotational matrices to the expansion coefficients. This method is computationally less expensive than the concurrent Cartesian correlation scheme. Hydrophobicity is mapped onto the protein surface by assigning to the surface regions values 1 and zero, for those belonging to hydrophobic amino acids residues and otherwise, respectively. Obtained results suggest that the method is feasible and that correlating hydrophobicity may be helpful in better ranking docked complexes, albeit more testing is needed.

Izvorni jezik
Engleski

Znanstvena područja
Biologija, Računarstvo



POVEZANOST RADA


Projekt / tema
036-0362214-1987 - Modeliranje kompleksnih sustava (Branko Jeren, )
098-1191344-2860 - Proučavanje biomakromolekula računalnim metodama i razvoj novih algoritama (Sanja Tomić, )

Ustanove
Fakultet elektrotehnike i računarstva, Zagreb,
Institut "Ruđer Bošković", Zagreb