Εξειδίκευση τύπου :	Άρθρο σε επιστημονικό περιοδικό
Τίτλος:	X-ray sequence ambiguities of Sclerotium rolfsii lectin resolved by mass spectrometry
Δημιουργός/Συγγραφέας:	Sathisha, G. J. Prakash, Y. K. Subrahmanya Chachadi, V. B. Nagaraja, N. N. Inamdar, S. R. [EL] Λεωνίδας, Δημήτρης Δ.[EN] Leonidas, Demetres D. Savithri, H. S. Swamy, B. M.
Εκδότης:	Springer Wien
Τόπος έκδοσης:	NEW YORK
Ημερομηνία:	2008-08
Γλώσσα:	Αγγλικά
ISSN:	0939-4451
DOI:	10.1007/s00726-007-0624-y
Περίληψη:	X-ray crystallography, although a powerful technique for determining the three-dimensional structure of proteins, poses inherent problems in assigning the primary structure in residues Asp/Asn and Glu/Gln since these cannot be distinguished decisively in the electron density maps. In our recently published X-ray crystal structure of the Sclerotium rolfsii lectin (SRL) at 1.1 angstrom resolution, amino acid sequence was initially deduced from the electron density map and residues Asp/Asn and Glu/Gln were assigned by considering their hydrogen bonding potential within their structural neighborhood. Attempts to verify the sequence by Edman sequencing were not successful as the N terminus of the protein was blocked. Mass spectrometry was applied to verify and resolve the ambiguities in the SRL X-ray crystal structure deduced sequence. From the Matrix assisted laser desorption/ionization time-of-flight-mass spectrometry (MALDI TOF-MS) and liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) analysis of tryptic and chymotryptic peptides of SRL, we could confirm and correct the sequence at five locations with respect to Asp/Asn and Glu/Gln. Analysis data also confirmed the positions of Leu/Ile, Gln/Lys residues and the sequence covering 118 of the total 141 residues accounting to 83.68% of the earlier deduced sequence of SRL.
Τίτλος πηγής δημοσίευσης:	Amino Acids
Τόμος/Κεφάλαιο:	35
Τεύχος:	2
Σελίδες:	309-320
Θεματική Κατηγορία:	[EL] Βιοχημεία[EN] Biochemistry
Λέξεις-Κλειδιά:	Sclerotium rolfsii lectin amino acid sequence mass spectrometry protein crystal structure
Αξιολόγηση από ομότιμους (peer reviewed):	Ναι
Κάτοχος πνευματικών δικαιωμάτων:	© SPRINGER
Ηλεκτρονική διεύθυνση περιοδικού (link) :	http://www.springer.at/amino_acids
ΙΒΦΧΒ: αρχειακή συλλογή:	Ινστιτούτο Οργανικής και Φαρμακευτικής Χημείας (ΙΟΦΧ) (έως 2012)
Εμφανίζεται στις συλλογές:	Ινστιτούτο Χημικής Βιολογίας - Επιστημονικό έργο