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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.
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 ...
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.
Macroscopic examples of chirality are found in the plant kingdom, the animal kingdom and all other groups of organisms. A simple example is the coiling direction of any climber plant, which can grow to form either a left- or right-handed helix. In anatomy, chirality is found in the imperfect mirror image symmetry of many kinds of animal bodies.
An example of a molecule that does not have a mirror plane or an inversion and yet would be considered achiral is 1,1-difluoro-2,2-dichlorocyclohexane (or 1,1-difluoro-3,3-dichlorocyclohexane). This may exist in many conformers ( conformational isomers ), but none of them has a mirror plane.
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.
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?
In statistical mechanics, the Zimm–Bragg model is a helix-coil transition model that describes helix-coil transitions of macromolecules, usually polymer chains. Most models provide a reasonable approximation of the fractional helicity of a given polypeptide; the Zimm–Bragg model differs by incorporating the ease of propagation (self-replication) with respect to nucleation.