The temperature dependence of amino acid hydrophobicity data is related to the genetic coding algorithm for complementary (sense and antisense) peptide interactions

Nikola Štambuk; Paško Konjevoda

doi:10.1016/j.dib.2020.105392

The temperature dependence of amino acid hydrophobicity data is related to the genetic coding algorithm for complementary (sense and antisense) peptide interactions

Data Brief. 2020 Mar 7:30:105392. doi: 10.1016/j.dib.2020.105392. eCollection 2020 Jun.

Authors

Nikola Štambuk¹, Paško Konjevoda²

Affiliations

¹ Centre for Nuclear Magnetic Resonance, Ruđer Bošković Institute, Bijenička cesta 54, HR-10000 Zagreb, Croatia.
² Laboratory for Epigenomics, Division of Molecular Medicine, Ruđer Bošković Institute, Bijenička cesta 54, HR-10000 Zagreb, Croatia.

Abstract

We present the data concerning the clustering of sense and antisense amino acid pairs into polar, nonpolar and neutral groups, as measured using hydrophobicity parameter-logarithmic equilibrium constants (Log₁₀ K_w>c)-at 25 °C and 100 °C (Wolfenden et al., 2015). The Log₁₀ K_w>c, values, of the complementary amino acid pairs are strongly correlated to the central (2nd) purine base of the mRNA codon and the complementary pyrimidine base of the tRNA anticodon. Clustering of amino acids is temperature independent with regard to the direction of translation (3' → 5' or 5' → 3'). The Log₁₀ K_w>c discriminate between artificial Hecht α- and β-protein datasets at 25 °C and 100 °C. Interpretation of this data may be found in the research article entitled "Determining amino acid scores of the genetic code table: complementarity, structure, function and evolution" (Štambuk and Konjevoda, 2020).

Keywords: Amino acid; Genetic code; Hydrophobicity; Peptide interaction; Temperature.