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Pregled bibliografske jedinice broj: 564503

Systematic comparison of crystal and NMR protein structures deposited in the protein data bank


Šikić, Kresimir; Tomić, Sanja; Carugo, Oliviero
Systematic comparison of crystal and NMR protein structures deposited in the protein data bank // The open biochemistry journal, 4 (2010), 83-95 doi:10.2174/1874091X01004010083 (podatak o recenziji nije dostupan, članak, znanstveni)


Naslov
Systematic comparison of crystal and NMR protein structures deposited in the protein data bank

Autori
Šikić, Kresimir ; Tomić, Sanja ; Carugo, Oliviero

Izvornik
The open biochemistry journal (1874-091X) 4 (2010); 83-95

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Protein structure ; NMR ; crystal structure

Sažetak
Nearly all the macromolecular three-dimensional structures deposited in Protein Data Bank were determined by either crystallographic (X-ray) or Nuclear Magnetic Resonance (NMR) spectroscopic methods. This paper reports a systematic comparison of the crystallographic and NMR results deposited in the files of the Protein Data Bank, in order to find out to which extent these information can be aggregated in bioinformatics. A non-redundant data set containing 109 NMR - X-ray structure pairs of nearly identical proteins was derived from the Protein Data Bank. A series of comparisons were performed by focusing the attention towards both global features and local details. It was observed that: (1) the RMDS values between NMR and crystal structures range from about 1.5 A to about 2.5 A ; (2) the correlation between conformational deviations and residue type reveals that hydrophobic amino acids are more similar in crystal and NMR structures than hydrophilic amino acids ; (3) the correlation between solvent accessibility of the residues and their conformational variability in solid state and in solution is relatively modest (correlation coefficient = 0.462) ; (4) beta strands on average match better between NMR and crystal structures than helices and loops ; (5) conformational differences between loops are independent of crystal packing interactions in the solid state ; (6) very seldom, side chains buried in the protein interior are observed to adopt different orientations in the solid state and in solution.

Izvorni jezik
Engleski

Znanstvena područja
Fizika



POVEZANOST RADA


Projekt / tema
098-1191344-2860 - Proučavanje biomakromolekula računalnim metodama i razvoj novih algoritama (Sanja Tomić, )

Ustanove
Institut "Ruđer Bošković", Zagreb

Časopis indeksira:


  • Scopus


Uključenost u ostale bibliografske baze podataka:


  • CA Search (Chemical Abstracts)
  • EMBASE (Excerpta Medica)
  • CABI, PubMed Central, PubMed, DOAJ, Open J-Gate, Genamics JournalSeek, MediaFinder®-Standard Periodical Directory, Portico, PubsHub, J-Gate


Citati