26 research outputs found
Domain structure in high molecular weight high mobility group nonhistone chromatin proteins
Two related structural genes coding two homologous serine proteases in the Bacillus subtilis genome
Anharmonic Behavior in the Multisubunit Protein Apoferritin as Revealed by Quasi-Elastic Neuton Scattering
Quasi-elastic neutron scattering (QENS) has been used to study the deviation from Debye-law harmonic
behavior in lyophilized and hydrated apoferritin, a naturally occurring, multisubunit protein. Whereas analysis
of the measured mean squared displacement (msd) parameter reveals a hydration-dependent inflection above
240 K, characteristic of diffusive motion, a hydration-independent inflection is observed at 100 K. The
mechanism responsible for this low-temperature anharmonic response is further investigated, via analysis of
the elastic incoherent neutron scattering intensity, by applying models developed to describe side-group motion
in glassy polymers. Our results suggest that the deviation from harmonic behavior is due to the onset of
methyl group rotations which exhibit a broad distribution of activated processes (Ea,ave ) 12.2 kJ · mol-1, σ
) 5.0 kJ · mol-1). Our results are likened to those reported for other proteins
Evolutionary conservation of chymotrypsinogen gene: Genomic analysis and protein modeling
Evaluation of intraaxial enhancing brain tumors on magnetic resonance imaging: intraindividual crossover comparison of gadobenate dimeglumine and gadopentetate dimeglumine for visualization and assessment, and implications for surgical intervention
Secretin and VIP-stimulated adenylate cyclase from rat heart. I. General properties and structural requirements for enzyme activation
Membrane adenylate cyclase from rat heart was activated by the two gut peptides secretin and vasoactive intestinal peptide (VIP), glucagon, and the beta-adrenergic drug isoproterenol, in the presence of guanosine 5'-triphosphate (GTP). With all the stimuli tested, the optimal magnesium concentration was 5 mM, i.e. in excess over the 0.5 mM ATP substrate concentration and 0.01 mM GTP used as cofactor. Under these conditions, half-maximal adenylate cyclase activation with glucagon, secretin, and VIP was achieved at concentrations of 0.5, 0.5 and 1.0 microM, respectively. Data obtained with the secretin (7--27) fragment, a secretin antagonist, indicate that secretin and VIP acted on the same binding sites, which differed from glucagon binding sites. Structural requirements for secretin activation of cardiac adenylate cyclase were evaluated by comparing the potency and efficacy of parent peptides and synthetic analogs. The gastric inhibitory peptide GIP was inactive. When using 13 mono-or bi-substituted analogs, it appeared that amino acids in positions 1, 2, 3, 4 and 6 were of major importance while those in position 5 and 11 played a relatively minor role.SCOPUS: ar.jinfo:eu-repo/semantics/publishe
Comparison of gadobenate dimeglumine (Gd-BOPTA) with gadopentetate dimeglumine (Gd-DTPA) for enhanced MR imaging of brain and spine tumours in children
SCOPUS: ar.jinfo:eu-repo/semantics/publishe