Applying rigid transformation protocols, population of the detect

Applying rigid transformation protocols, population of the detected domain building models with an average root mean square deviation from native structures of 2.3 angstrom and an average template

modeling score from native structures of 0.43 has been obtained. The fold detection algorithm here proposed yields more accurate results than previously proposed methods, predicting structural homology also for proteins sharing less than 20% sequence identity. Our tools are freely available at (c) 2012 Elsevier Ltd. All rights reserved.”
“Methionine adenosyltransferase from Euglena gracilis (MATX) is a recently discovered member of the MAT family of proteins that synthesize S-adenosylmethionine. Heterologous overexpression of MATX in Escherichia coli rendered the protein mostly in inclusion bodies under all conditions tested. Therefore, a refolding and purification procedure selleck inhibitor from these aggregates was developed to characterize the enzyme. Maximal recovery was obtained using inclusion bodies devoid of extraneous proteins learn more by washing under mild urea (2 M) and detergent (5%) concentrations. Refolding was achieved in two steps following solubilization

in the presence of Mg(2+); chaotrope dilution to <1 M and dialysis under reducing conditions. Purified MATX is a homodimer that exhibits Michaelis kinetics with a V(max) of 1.46 mu mol/min/mg and K(m) values of approximately 85 and 260 mu M for methionine and ATP, click here respectively. The activity is dependent on Mg(2+) and K(+) ions, but is not stimulated by dimethylsulfoxide. MATX exhibits tripolyphosphatase activity that is stimulated in the presence of S-adenosylmethionine. Far-UV circular dichroism revealed beta-sheet and random coil as the main secondary structure elements of the protein. The high level of sequence conservation allowed construction of a structural model that preserved the main features of the MAT family,

the major changes involving the N-terminal domain. (C) 2011 Elsevier Inc. All rights reserved.”
“A predictive mathematical model of the transition from the G2 phase in the cell cycle to mitosis (M) was constructed from the known interactions of the proteins that are thought to play significant roles in the G2 to M transition as well as the DNA damage- induced G2 checkpoint. The model simulates the accumulation of active cyclin B1/Cdk1 (MPF) complexes in the nucleus to activate mitosis, the inhibition of this process by DNA damage, and transport of component proteins between cytoplasm and nucleus. Interactions in the model are based on activities of individual phospho-epitopes and binding sites of proteins involved in G2/M. Because tracking phosphoforms leads to combinatorial explosion, we employ a rule-based approach using the BioNetGen software.

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