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The chirality of a molecule that has a helical, propeller, or screw-shaped geometry is called helicity [5] or helical chirality. [6] [7] The screw axis or the D n, or C n principle symmetry axis is considered to be the axis of chirality. Some sources consider helical chirality to be a type of axial chirality, [7] and some do not.
Consider, for example, a baseball, pitched as a gyroball, so that its spin axis is aligned with the direction of the pitch. It will have one helicity with respect to the point of view of the players on the field, but would appear to have a flipped helicity in any frame moving faster than the ball.
Helicity is a pseudo-scalar quantity: it changes sign under change from a right-handed to a left-handed frame of reference; it can be considered as a measure of the handedness (or chirality) of the flow. Helicity is one of the four known integral invariants of the Euler equations; the other three are energy, momentum and angular momentum.
Since the helicity of massive particles is frame-dependent, it might seem that the same particle would interact with the weak force according to one frame of reference, but not another. The resolution to this paradox is that the chirality operator is equivalent to helicity for massless fields only, for which helicity is not frame-dependent. By ...
Helicity may refer to: Helicity (fluid mechanics), the extent to which corkscrew-like motion occurs; Helicity (particle physics), the projection of the spin onto the ...
The two-component helicity eigenstates satisfy ^ (^) = (^) where are the Pauli matrices, ^ is the direction of the fermion momentum, = depending on whether spin is pointing in the same direction as ^ or opposite.
Examples of mesons include the pion, kaon, and the J/ψ. In quantum hadrodynamics , mesons mediate the residual strong force between nucleons. At one time or another, positive signatures have been reported for all of the following exotic mesons but their existences have yet to be confirmed.
Protein folding problem: Is it possible to predict the secondary, tertiary and quaternary structure of a polypeptide sequence based solely on the sequence and environmental information? Inverse protein-folding problem: Is it possible to design a polypeptide sequence which will adopt a given structure under certain environmental conditions?