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Matter always remains the guise and result of energetic interactions.
The stagnation line where the most energetic interactions take place is inspected carefully.
Proteins are polymeric molecules with many degrees of conformational freedom whose internal energetic interactions are typically screened to small distances.
These results indicate that inter-residue energetic interactions do not control conformational diffusion in unfolded states, even under folding conditions.
However, in some proteins, specifics of local energetic interactions modulate domain-swapping and these need to be added to the symmetrized SBMs.
Various components of energetic interactions have been examined in detail in order to gain a better insight into interactions between bulk structure and the film.
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Here, we define phreatomagmatic eruptions as including activities caused by weakly energetic interaction of magma and external water.
The preferential energetic interaction of MgCl2 with glycerol and water modifies the phase equilibrium, thereby eliminating the azeotrope of 2M2P + water system.
Since there is no energetic interaction with the filler, no adsorption transition is observed, but the chains tend to wrap around the filler once the gyration radius becomes comparable to the filler radius.
Aiming to predict the antibody-binding regions of a protein, we investigate a new approach based on the integrated analysis of the dynamical and energetic properties of antigens, to identify nonoptimized, low-intensity energetic interaction networks in the protein structure isolated in solution.
Ligand binding is generally known as a local process where the binding molecule finds a suitable location on the protein that has the right shape and the favorable energetic interaction [1].
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