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Chirality is the most intriguing yet essential facet of nature, governing life’s biochemical processes and precision. It can be observed from a snail shell pattern in a macroscopic world to an amino acid, the minutest building block of life. Most of the snails around the world have right-coiled shells because of the intrinsic chirality in their genes. All the amino acids present in the human body exist in an enantiomerically pure state, except for glycine - the sole achiral amino acid.
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Chirality is a term that describes the lack of mirror symmetry in an object. In other words, chiral objects cannot be superposed on their mirror images. For example, our feet are chiral, as the mirror image of the left foot, the right foot, cannot be superposed on the left foot.
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Chirality in a quaternionic representation of the genetic code.

C Manuel Carlevaro1, Ramiro M Irastorza2, Fernando Vericat3

  • 1Instituto de Física de Líquidos y Sistemas Biológicos, 59 Nro. 789, 1900 La Plata, Argentina; Universidad Tecnológica Nacional, Facultad Regional Buenos Aires, Mozart Nro. 2300, C14071VT Buenos Aires, Argentina.

Bio Systems
|July 6, 2016
PubMed
Summary
This summary is machine-generated.

This study updates a quaternionic representation of the genetic code to include chirality in nucleotide bases and amino acids, enabling protein structure prediction and exploring chiral genetic code evolution.

Keywords:
Genetic code representationHomochiral protein foldingHomochirality

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Area of Science:

  • * Bioinformatics and Computational Biology
  • * Structural Biology
  • * Biophysics

Background:

  • * The genetic code's fundamental role in translating nucleotide sequences into amino acid chains is well-established.
  • * Previous work established a quaternionic representation of the genetic code, preserving its degeneracy.
  • * Incorporating chirality is crucial for a comprehensive understanding of molecular interactions and biological systems.

Purpose of the Study:

  • * To update the existing quaternionic genetic code representation by incorporating chirality of nucleotide bases and amino acids.
  • * To develop an algorithm for predicting protein tertiary structure from primary sequence using chiral quaternions.
  • * To explore hypothetical evolutionary pathways of chiral genetic codes.

Main Methods:

  • * Extension of a prior quaternionic representation of the genetic code to include chirality.
  • * Association of nucleotide bases and amino acids with specific integer quaternions of norm 7.
  • * Development of an algorithm utilizing 'type quaternions' and 'order quaternions' for protein folding prediction.
  • * Partitioning of quaternions to represent D- and L-enantiomers of nucleotide bases and amino acids.

Main Results:

  • * A novel quaternionic framework successfully incorporates chirality into the genetic code representation.
  • * The framework enables the prediction of protein tertiary structure from primary sequence.
  • * Two diagrams illustrate hypothetical evolutionary paths for chiral genetic codes (D-nucleotides/L-amino acids and L-nucleotides/D-amino acids).
  • * Functions were defined to assign chiral amino acid type quaternions based on base triplets.

Conclusions:

  • * The updated quaternionic representation provides a powerful tool for studying the genetic code and protein structure.
  • * The incorporation of chirality offers new insights into molecular recognition and biological system evolution.
  • * The developed algorithm demonstrates potential for advancing protein structure prediction methodologies.