Bound-state resonances and interaction potential of helium scattered by graphite (0001)

1979 ◽  
Vol 20 (10) ◽  
pp. 3957-3969 ◽  
Author(s):  
G. Boato ◽  
P. Cantini ◽  
C. Guidi ◽  
R. Tatarek ◽  
G. P. Felcher
Keyword(s):  
Interaction Potential ◽  
Bound State

scholarly journals The hyperon-nucleon interaction potential in the bound-state soliton model: the ΛN case

1999 ◽  
Vol 646 (1) ◽  
pp. 108-124
Author(s):  
G.L. Thomas ◽  
V.E. Herscovitz ◽  
C.L. Schat ◽  
N.N. Scoccola
Keyword(s):  
Interaction Potential ◽  
Bound State ◽  
Nucleon Interaction ◽  
Soliton Model

Nanoparticles in Antivirus Therapy

2013 ◽  
Vol 854 ◽  
pp. 149-155 ◽  
Author(s):  
Mikhail Lokshyn ◽  
V. Lozovski ◽  
V.S. Lysenko ◽  
V. Piatnytsia ◽  
M. Spivak ◽  
...  
Keyword(s):  
Interaction Potential ◽  
Viral Particle ◽  
Bound State ◽  
Activity Inhibition ◽  
Nonspecific Interaction ◽  
Virus Activity ◽  
Linear And Nonlinear

The new mechanism of the virus activity inhibition is proposed. The idea is based on the nonspecific interaction between the viral particle and nanoparticles forming a stable bound state. The formation of the interaction potential between the virus and nanoparticles is caused by the presence of both linear and nonlinear polarizabilities, leading to the emergence of the attractive and repulsive parts of the potential, respectively.

He-Ag(110) interaction potential by new bound-state-resonance measurements

1986 ◽  
Vol 34 (8) ◽  
pp. 5897-5899 ◽  
Author(s):  
M. G. Dondi ◽  
L. Mattera ◽  
S. Terreni ◽  
F. Tommasini ◽  
U. Linke
Keyword(s):  
Interaction Potential ◽  
Bound State ◽  
State Resonance

Bound state resonances and related interaction potential for atomic hydrogen on NaCl(001)

1982 ◽  
Vol 120 (1) ◽  
pp. L417-L424 ◽  
Author(s):  
L. Baetz ◽  
H. Hoinkes ◽  
H. Wilsch
Keyword(s):  
Interaction Potential ◽  
Atomic Hydrogen ◽  
Bound State

CRYO-Electron Microscopy of the Acto-Myosin-ATP Complex

1990 ◽  
Vol 48 (1) ◽  
pp. 248-249
Author(s):  
John Trinickt ◽  
Howard White
Keyword(s):  
Electron Microscopy ◽  
Atp Hydrolysis ◽  
Myosin Head ◽  
Bound State ◽  
Cross Linking ◽  
Weakly Bound ◽  
Cryo Electron Microscopy ◽  
Myosin Subfragment 1 ◽  
Attached State ◽  
High Fraction

The primary force of muscle contraction is thought to involve a change in the myosin head whilst attached to actin, the energy coming from ATP hydrolysis. This change in attached state could either be a conformational change in the head or an alteration in the binding angle made with actin. A considerable amount is known about one bound state, the so-called strongly attached state, which occurs in the presence of ADP or in the absence of nucleotide. In this state, which probably corresponds to the last attached state of the force-producing cycle, the angle between the long axis myosin head and the actin filament is roughly 45°. Details of other attached states before and during power production have been difficult to obtain because, even at very high protein concentration, the complex is almost completely dissociated by ATP. Electron micrographs of the complex in the presence of ATP have therefore been obtained only after chemically cross-linking myosin subfragment-1 (S1) to actin filaments to prevent dissociation. But it is unclear then whether the variability in attachment angle observed is due merely to the cross-link acting as a hinge.We have recently found low ionic-strength conditions under which, without resorting to cross-linking, a high fraction of S1 is bound to actin during steady state ATP hydrolysis. The structure of this complex is being studied by cryo-electron microscopy of hydrated specimens. Most advantages of frozen specimens over ambient temperature methods such as negative staining have already been documented. These include improved preservation and fixation rates and the ability to observe protein directly rather than a surrounding stain envelope. In the present experiments, hydrated specimens have the additional benefit that it is feasible to use protein concentrations roughly two orders of magnitude higher than in conventional specimens, thereby reducing dissociation of weakly bound complexes.

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