Asymmetric time MTOCs conserves evolution & evolutionary conserved Yuan Qi nonlocal noncommutative

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Establishing differences in the properties of L- and D-tryptophan (Trp) which are part
of various proteins, enzymes, and receptors is an important fundamental and practical
problem, as the optical isomers themselves are identical in physicochemical properties,
while proteins containing L- and D-isomers of amino acids, in particular, Trp, are dramatically
different [1]. Thus, chiral inversion, which as is known, occurs during aging of living
organisms and leads to the replacement in a number of proteins L-isomers of amino acids
with D-analogs, is currently considered one of the main causes of Alzheimer’s, Parkinson’s,
type II diabetes, and a number of other pathological conditions [1, 2]."
a chiral acceptor, for studying the optical configuration influence
on the photoinduced elementary processes—electron transfer (ET) and Förster
resonance energy transfer (RET). As Trp is one of the few fluorescent amino acids, a set
of physicochemical methods can be used in the study of the comparative reactivity of its
optical isomers in elementary processes [4]. Meanwhile, the joint application of chemically
induced dynamic nuclear polarization (CIDNP) and fluorescence spectroscopy techniques
to study photoinduced charge transfer processes in a number of dyads

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