Abstract
A new mode of interaction, to be termed “chiral interaction”, is proposed between chiral molecules such as proteins and polar solvents (H2O). Such a mode of interaction is well-recognized for macroscopic chiral devices, such as windmills or electric cells, and various media, such as wind or electrolyte. This mode of interaction requires several structural ingredients, all possessed by proteins, and its source is in ionic motion in the solvent. Such an interaction exists only for chiral objects or molecules and therefore possesses several peculiar and uncommon features, which may be of special biological significance. From a thermodynamical viewpoint this phenomenon is non-ergodic and time-irreversible, and therefore does not obey the principle of detailed balance. The energy content of this interaction is rather small and therefore it is to be regarded as a subthermal organization. Chiral interaction appears in the form of an intrinsic flow of perturbation or currents throughout the molecule and hence it is not easily observable. Two experiments are proposed for its observation. One is direct and the other is based on an assumption that couples chiral interaction with enzymatic activity. A model is proposed that links this interaction with the natural selection of the L-enantiomer of amino acids via the magnetic field of the earth. Several structural and other properties may obtain biological significance via the concept of chiral interaction. It is conjectured that chiral interaction may play a significant role in the control of protein activity.
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References
This is so except for glycine, which is achiral.
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