Search Results - "Magri, Ermes"

A possible solvent effect of adenosine diphosphate influences the binding of 1, N6 ethenoadenosine diphosphate to myosin from skeletal muscle by Grazi, Enrico, Cintio, Orietta, Magri, Ermes, Trombetta, Giorgio

“…Skeletal muscle myosin displays two independent and equivalent binding sites for 1, N 6 ethenoadenosine diphosphate, with a dissociation constant of 24.7 μM…”
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Osmotic properties of the calcium-regulated actin filament by Schwienbacher, Christine, Magri, Ermes, Trombetta, Giorgio, Grazi, Enrico

“…The diameter of the actin filament decreases with an increase of the protein osmotic pressure. This phenomenon is accompanied by a decrease of the angle…”
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Anomalous binding of MgADP to myosin of skeletal muscle by Grazi, E, Cintio, O, Magri, E, Trombetta, G

“…Binding of adenosine diphosphate to skeletal muscle myosin was studied using a range of concentrations from 0 to 2 mM. Up to 0.2 mM adenosine diphosphate two…”
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The stiffness of the crossbridge is a function of the intrinsic protein osmotic pressure generated by the crossbridge itself by Grazi, Enrico, Magri, Ermes, Schwienbacher, Christine, Trombetta, Giorgio

“…A model is presented that makes it possible to determine the stiffness of the crossbridge from protein osmotic stress experiments. The model was elaborated…”
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Dissecting the free energy of formation of the 1:1 actomyosin complex by Grazi, Enrico, Adami, Raffaella, Cintio, Orietta, Cuneo, Paola, Magri, Ermes, Trombetta, Giorgio

“…The behaviour of solutions of pure myosin, of pure F-actin and of the equimolar mixture of myosin and of F-actin is studied. It is found that the chemical…”
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Reversible Inactivation of Myosin Subfragment-1 Activity by Mechanical Immobilization: A Reappraisal by Grazi, Enrico, Cintio, Orietta, Magri, Ermes, Trombetta, Giorgio

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The stiffness of the crossbridge is a function of the intrinsic protein osmotic pressure generated by the crossbridge itself by Grazi, Enrico, Magri, Ermes, Schwienbacher, Christine, Trombetta, Giorgio

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Osmotic stress is the main determinant of the diameter of the actin filament by Grazi, E, Schwienbacher, C, Magri, E

“…The diameter of the actin filament is influenced by osmotic stress, being 9.0 nm at 1 x 10(5) dynes/cm2 and 6.8 nm at 9.00 x 10(6) dynes/cm2. At 1.81 x 10(5)…”
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Diffusion hindrance and geometry of filament crossings account for the complex interactions of F-actin with .alpha.-actinin from chicken gizzard by Grazi, Enrico, Cuneo, Paola, Magri, Ermes, Schwienbacher, Christine, Trombetta, Giorgio

“…The interaction of alpha-actinin from chicken gizzard with F-actin is quite complex. The apparent dissociation constant, C, increases with the increase of…”
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Osmotic Properties of Myosin Subfragment 1: Implications of the Mechanism of Muscle Contraction by Grazi, E., Magri, E., Schwienbacher, C., Trombetta, G.

“…The osmotic behavior of myosin subfragment 1 was studied at 22°C and pH 7.45 in 0.1 m KCl, 2 m m MgCl 2, and 10 m m triethanolamine or in 25 m m phosphate, 2 m…”
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The control of cellular motility and the role of gelsolin by Grazi, Enrico, Magri, Ermes, Cuneo, Paola, Cataldi, Alberto

“…Solation of actin gel by gelsolin is much less efficient in the presence of a high concentration of macromolecular solutes. The rigidity of the gel formed by…”
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Actin may contribute to the power stroke in the binary actomyosin system by Grazi, E, Magri, E, Schwienbacher, C, Trombetta, G

“…At the physiological protein osmotic pressure, the angle formed between the long axis of the actin monomer and the pointed end of the filament axis is roughly…”
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Myofibrils of skeletal muscle: The activity coefficient of orthophosphate by Grazi, Enrico, Adami, Raffaella, Magri, Ermes, Trombetta, Giorgio, Frassinefi, Chiara

“…In the myofibrils of skeletal muscle, at 22°C, pH 7.1 and at the physiological protein osmotic pressure of 1.8×105 dynes/cm2, orthophosphate behaves quite…”
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Preferential binding of α-actinin to actin bundles by Grazi, Enrico, Cuneo, Paola, Magri, Ermes, Schwienbacher, Christine

“…At 37°C, the α-actinin-F-actin binding isotherm is anomalous. In 6.7% polyethylene glycol 6000, concomitantly with the formation of actin bundles, the binding…”
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The actin gelling activity of chicken gizzard α-actinin at physiological temperature is triggered by water sequestration by Grazi, Enrico, Trombetta, Giorgio, Magri, Ermes, Cuneo, Paola

“…At 37°C, in the presence of 6% ( w v ) polyethylene glycol 6000, 30 nM α-actinin from chicken gizzard induces the gelation of 12 μM actin. Static measurement…”
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A Model Relating Protein Osmotic Pressure to the Stiffness of the Cross‐Bridge Components and the Contractile Force of Skeletal Muscle by Grazi, Enrico, Magri, Ermes, Schwienbacher, Christine, Trombetta, Giorgio

“…We have modeled the effect of protein osmotic pressure on the orientation of the monomer in F‐actin, in tropomyosin‐F‐actin, in the myosin subfragment‐1…”
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Protein cross talking through osmotic work: the free energy of formation of the MgADP-myosin complexes at the muscle protein osmotic pressure by Grazi, Enrico, Cuneo, Paola, Magri, Ermes, Adami, Raffaella, Trombetta, Giorgio

“…A method is presented to determine the energy of formation of the myosin-ADP complexes at the muscle protein osmotic pressure. It is found that, at 18 kP, the…”
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The Osmotic Properties and Free Energy of Formation of the Actomyosin Rigor Complexes from Rabbit Muscle by Magri, Ermes, Cuneo, Paola, Trombetta, Giorgio, Grazi, Enrico

“…We have studied the osmotic properties of the calcium‐regulated actomyosin complexes from skeletal muscle at the protein osmotic pressure of 18 kPa and at…”
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Phosphorylation of actin and removal of its inhibitory activity on pancreatic DNAase I by liver plasma membranes by Grazi, Enrico, Magri, Ermes

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Studies on the polymerisation of actin: a rapid method for the separation of the monomeric from the polymeric species by Grazi, Enrico, Magri, Ermes

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